ࡱ>       ~` bjbj ۩+O    D D D $h AAAP BTtDh <DFLF"FFFLL LFHHHHHH$h+lD mRLLmRmRl  FFCAi`i`i`mR^ F(D FFi`mRFi`i`JaD خF8F Q!=AXBdW06\^خخzD REMVNi`OSPLL1M =Mll `^EMEMEMmRmRmRmRh h h 2,<h h h ,<h h h        SHAPE \* MERGEFORMAT  Preliminary Examination Report submitted by Carl Weisbecker September 26th, 2008 Research Advisor: Professor Athula Attygalle Center for Mass Spectrometry Stevens Institute of Technology  Do ECD and ETD proceed by the same mechanism in peptide cations? Carl Weisbecker Stevens institute of Technology, Hoboken, Castle Point on Hudson, NJ 07030 Abstract Processes by which gaseous peptide ions dissociate are an important topic in the field of mass spectrometry, because the understanding of these dissociation mechanisms is essential to the application of tandem mass spectrometry for determination of the amino acid sequence in peptides. Peptide structural characterization leads further to the characterization of the primary structure of proteins. Gaseous peptide cations frequently are prepared by ionization of a solution of the peptide (M) in an electrospray interface, which typically generates multiply charged protonated even-electron ions of the form [M + nH]n+. Methods such as collision induced dissociation (CID) are then applied to cause dissociation of the peptide cations by heterolytic cleavage of amide bonds. The dissociation products comprise a series of complementary b- and y-type ions that can be used to determine the amino acid sequence in the peptide. Electron capture dissociation (ECD) and electron transfer dissociation (ETD) are two closely related new dissociation methods that yield more extensive sequence information from peptides. ECD is initiated by interaction of cations with low energy electrons; whereas, ETD is initiated by the transfer of an electron from an anion or neutral molecule. Peptide cations [M + nH]n+ subjected to these methods are partially reduced to form radical cations of the form [M + nH](n-1)+. Dissociation of these radical cations produces a complementary series of c- and z-type ions from homolytic cleavage of N-C( bonds. The dissociation mechanism differs fundamentally from the previously described CID of even-electron ions. In the critique, I will describe the mechanisms that have been proposed to explain the dissociation products of peptide radical cations by ECD and ETD. The ECD and ETD processes have been assumed to proceed by essentially the same mechanism after the cation reduction to form the [M + nH](n-1)+ radical cation. In the proposal, I will argue that a better understanding of the dissociation mechanism (or mechanisms) involved could be obtained by focusing on specific cases where the mechanisms of ECD and ETD might be shown to differ. Literature for the Critique Zubarev, R. A.; Haselmann, K. F.; Budnik, B.; Kjeldsen, F.; Jensen, F. Towards an understanding of the mechanism of electron-capture dissociation: a historical perspective and modern ideas, European J. Mass Spectrom., 2002, 8, 337. Sawicka, A.; Skurski, P.; Hudgins, R. R.; Simons, J. Model Calculations Relevant to Disulfide Bond Cleavage via Electron Capture influenced by Positively Charged Groups, J. Phys. Chem. B, 2003, 107, 13505. Sobczyk, M.;Neff, D.; Simons, J.Theoreticalstudyofthrough-spaceandthrough-bondelectrontransferwithinpositivelychargedpeptidesin the gas phase, Int.J. MassSpectrom., 2008, 269,149. Gunawardena, H.P.; Gorenstein,L.; Erickson, D.E.;Xia,Y.; McLuckey,S.A. Electrontransferdissociationofmultiplyprotonatedandfixedchargedisulfide linkedpolypeptides, Int.J. MassSpectrom.,2007, 265, 130. Anusiewicz, I.; Berdys-Kochanska, J.; Simons, J. Electron Attachment Step in Electron Capture Dissociation (ECD) and Electron Transfer Dissociation (ETD) , J. Phys. Chem. A, 2005, 109, 5801. Syrstad, E.A.; Ture ek, F. Towardageneralmechanismofelectroncapture dissociation ,J. Am.Soc.MassSpectrom.,2005, 16,208. Ture ek, F. N-C( Bond Dissociation Energies and Kinetics in Amide and Peptide Radicals. Is the Dissociation a Non-Ergodic Process?, J. Am. Chem. Soc., 2003, 125, 5954. Introduction Background on Mass Spectrometry and Peptide Structural Characterization The primary structure of a peptide consists of a linear sequence of amino acids linked by amide bonds. Peptides and proteins may also have higher level structural features called secondary, tertiary, and quaternary structure. Techniques of nuclear magnetic resonance (NMR) and x-ray crystallography are often used to gain information about peptide and protein structure.1 These techniques are sometimes used in combination with computer simulations known as molecular dynamics.2 NMR and x-ray crystallography require large amounts of pure and highly concentrated samples. In cases where the sample is not available in abundance or is not easily crystallized, tandem mass spectrometry is an important ancillary technique of structural analysis. Techniques of liquid chromatography coupled to mass spectrometry (LC-MS) are also useful for the separation and analysis of mixtures of peptides.3 Mass spectrometry (MS) is a widely applied technology with demonstrated applications in proteonomics research due to its sensitivity, specificity, and speed of analysis. Fundamentally, MS measures the mass-to-charge ratio (m/z) and the relative abundance of peptides, proteins, and their fragments. Interfacing of MS with different chromatographic and ionization techniques has allowed very small amounts of biomolecules and even complete viruses to be investigated.4 The development of soft ionization techniques such as matrix-assisted laser desorption ionization (MALDI) and electrospray ionization (ESI) have aided these advances.5,6 Ionization of molecules in the vapor phase has traditionally been accomplished using techniques such as electron impact (EI) or chemical ionization (CI), but these techniques are ineffective to ionize proteins, peptides, and other fragile biomolecules, which cannot easily be transferred into the vapor phase intact. ESI is a common technique to prepare peptide cations for mass spectrometric analysis. ESI produces ions by spraying a sample solution through a narrow capillary to which a potential of several kilovolts is applied. The technique can be used to produce multiply charged ions. ESI of peptides typically produces even-electron ions bearing positive charge due to excess protons, which are attached to basic sites on the backbone or side chains.7 The Fourier transform ion cyclotron resonance mass spectrometer (FTICR-MS) is one type of high-end instrument that supports the capability to perform gas-phase reactions for structural analysis of large intact molecules. The FTICR-MS uses a combination of magnetic and electric fields to trap ions non-destructively under high vacuum conditions. Electromagnetic fields are used to manipulate the trapped ions and to investigate reactions.8 FTICR-MS has enabled a so-called top-down approach to protein structure characterization. The top-down approach consists of the accurate mass measurement of an ionized intact protein, followed by the application of tandem mass spectrometry for the structural analysis of the protein through analysis of its ionized peptide fragments.9 The alternative bottom-up approach requires that the protein is chemically cleaved (digested) into small peptide fragments in a solution prior to gas-phase ionization and mass spectroscopic analysis. Protein characterization in the bottom-up approach is based on mass measurements of gas-phase ions of digested peptide products.10 Background on Collision Induced Dissociation Collision induced dissociation (CID) is a fragmentation technique in which ions interact with neutral molecules in the vapor phase. Internal energy of the precursor ion is increased by the collisions with the vapor until dissociation occurs. CID is understood to be as slow-heating technique. The term slow-heating means that an increase of the internal energy in the ion becomes distributed throughout all available vibrational modes on a time scale much longer than the time scale of bond cleavage.11 After production of ions by ESI or other techniques, the precursor ion in a tandem mass spectrometry experiment is first isolated from among other ions in a process called mass selection. The selected ion is subjected to a dissociation technique. The resulting MS/MS or MSn spectrum will record the m/z and relative yields of charged dissociation products. Information about the sequence of amino acids in a peptide can be obtained whenever dissociation products result from cleavage of the peptide backbone. There are three main types of bond cleavage that can occur along the peptide backbone. The excess proton nearest the dissociating bond may be retained by either the N-terminal fragment or the C-terminal fragment. Fragments that retain the proton on the N-terminal side are designated a, b, or c, and fragments that retain a proton on the C-terminal side are designated x, y, or z according to a widely accepted nomenclature (Figure 1).12 Dissociation of an ion often occurs inside of a collision cell containing a dilute gas of neutral atoms, such as argon or helium. The dissociation products of the CID technique are predominantly b- and y- type ions that originate from heterolytic cleavage of peptide bonds.13  Fig. 1. Labeling of Peptide Dissociation Products Background on Electron Capture and Electron Transfer Dissociation ECD of multiply charged peptides and proteins results in extensive cleavage of bonds in the peptide backbone. The ECD process differs in several fundamental ways from the CID process.15 Whereas CID and related techniques proceed by heterolytic cleavage of peptide bonds, ECD proceeds by homolytic cleavage of the N-C( bond of the peptide backbone. Cleavage of disulfide bonds also occurs readily in ECD.16 Non-covalent interactions, such as hydrogen bonding may be preserved intact while stronger covalent bonds are cleaved.17 The dissociation products of ECD are mixtures of radical cations and even-electron ions. The overall process of electron capture dissociation (ECD) can be described by the following equations:14  The mechanism of ECD has widely been described as a non-ergodic process and thus contrasted with more classical dissociation mechanisms applicable to CID.18 There is significant doubt and ambiguity among researchers about this classification.19 Ergodicity refers to a process in which complete randomization of internal energy occurs within the molecule prior to its dissociation. Non-ergodicity, by contrast, implies that the recombination energy added to the peptide when it captures an electron is all or mostly directed into specific localized excitation and bond cleavage adjacent to an excitation site. The overall process of electron transfer dissociation (ETD) can be described by the following equations:20 Whereas ECD uses an electron gun as a source of electrons, ETD instead uses an anion or neutral molecule as an electron transfer agent. If the neutral precursor of the anion has a sufficiently low electron affinity, then a gas-phase anion cation reaction may occur resulting in charge reduction of the cation. The ECD technique previously described is exclusively implemented using an FTICR-MS instrument, which is a type of mass spectrometer that is expensive and not widely available. ETD has shown versatility and potential to be implemented more widely using quadrupole ion traps, which are less costly.21 The anionic transfer agents in ETD are typically small organic molecules with aromaticity, such as anthracene. One important difference between ETD and ECD is that the anion cation reaction between a multiply protonated peptide and a singly charged anion may also yield products associated with proton transfer.22 Abstraction of a proton from the peptide cation competes with donation of an electron: ETD has also recently been demonstrated using neutral electron transfer agents with low ionization potentials, such as monatomic cesium vapor.23 Critique of the Literature Review of the Literature Many of the experimental observations of ECD and ETD of peptides and proteins have been successfully explained by the hot hydrogen atom transfer mechanism, which is depicted in Scheme 1 for the cases of N-C( bond breaking and disulfide bond breaking.24 This mechanism has several key features. The electron is captured into an excited electronic state of a positively charged functional group, such a protonated amine of lysine. This excited state is often referred to in the literature as a Rydberg state. The electron loses energy and eventually inhabits the lowest unoccupied orbital associated with the charged functional group. The loss of the electron energy as it falls into its ground state is called the recombination energy. A hypervalent ammonium radical with an excess hydrogen atom is produced. The hydrogen atom dissociates rapidly and exothermically. It is described as hot due to a portion of recombination energy that it carries away with it in the form of kinetic energy. Capture of hydrogen by an amide carbonyl oxygen produces an aminoketyl radical, which activates an adjacent N-C( bond causing homolytic cleavage.26, 27 Capture of hydrogen by a disulfide group produces a thiasulfonium radical, which initiates homolytic cleavage of the disulfide bond.16, 28, 29  Scheme 1. Hot Hydrogen Atom Transfer Mechanisms for N-C( and Disulfide Bond Cleavage The research group of Zubarev attempted to advance understanding of the ECD mechanism by estimating the magnitude of the recombination energy.14 They estimated that the recombination energy associated with electron capture by a peptide cation falls in the range of 4 7 eV. They observed that this recombination energy exceeds the bond dissociation energy (BDE) of typical covalent bonds, which they estimated to be 3 - 4 eV. They thus confirmed that electron capture adds enough internal energy to a typical peptide cation to cause dissociation of at least one covalent bond. The group attempted to provide a theoretical description of the energetics of the hot hydrogen atom transfer mechanism using ab initio calculations on a model system consisting of N-methylacetamide (representing a fragment of a peptide) and protonated methylamine (representing a protonated amine group at the terminus of a lysine residue.) Their calculations of this model system are summarized in the energy level diagram below (Figure 2). Dissociation of the N-CH3 bond of acetamide has a high energy barrier and is rate determining, according to their calculation. Some observations are inconsistent with the hot hydrogen atom model. Hydrogen atoms with low energy (<1 eV) generated by other means have not been observed to spontaneously attach or fragment protonated peptides.30 The collisional excitation of disulfide groups with attached hydrogen atoms does not produce dissociation of the disulfide bond as would be expected according to the hot hydrogen atom model.28  Fig. 2. Calculated Energy Diagram of the Hot Hydrogen Atom Transfer Mechanism involving N-Methylacetamide and Methylammonium Cation (units of kJ/mol) The research group led by Simons has recently published several related papers in which they investigated various ECD and ETD mechanisms theoretically while reviewing important experimental work.31, 32 They cited cases in which experimental findings do not support the hot hydrogen atom transfer model of dissociation, and they used theoretical simulations of model structures to investigate alternative mechanisms of ECD and ETD. The group proposed a Coulombassisted direct attachment mechanism in which the presence of positively charged functional groups nearby in a multiply-charged cation stabilizes electron attachment (Scheme 2). Previous research has shown that direct electron attachment to a disulfide (* orbital is endothermic by approximately 1 eV. Direct electron attachment to an amide (* orbital is also endothermic by 2.5 eV.  Scheme 2. Coulomb Assisted Direct Attachment Mechanism The Simons group used a point-charge model to estimate Coulombic stabilization of an attached electron due to a neighboring positive charge. In the equation below, r is the distance between the positive charge and the attached electron (with units of .) The Coulombic potential energy (VC) is in units of electron-volts. q1 and q2 are the charges of the electron and positive charge: VC = (1/4((0) q1 q2 ( r = -14.4 ( r A single positive charge at a distance of 14.4 is thus estimated to lower the potential energy of an attached electron by 1 eV. The Coulombic interactions are additive; therefore, other positive charges in a multiply charged peptide ion contribute further to energy lowering. Experimental results of the Marshall group were cited as a case in which direct attachment can explain observations. ECD of synthetic peptides with the form shown below in Figure 3 were reported.16 A central disulfide bond is separated from two protonated lysines by a variable length spacer composed of alanine amino acids.  Fig. 3. Disulfide Linked Peptide with Two Terminal Protonated Amines There is good evidence that the conformation in the gas phase is an extended helix, as shown, rather than some other more compact structure.33 Significant disulfide cleavage was reported even for a structure in which the two lysine groups were estimated to be 30 distant from the disulfide bond. N-C( bond cleavage was observed only within the first four alanines closest to each lysine terminus. The Simons group observed that cleavage of the disulfide bond in these peptides appears inconsistent with the hot hydrogen atom transfer model, because the central disulfide linkage resides too far from the charge sites. They proposed that the mechanism of disulfide bond dissociation is more likely to be direct electron attachment to the disulfide bond. The Simons group considered intramolecular electron transfer mechanisms in which an electron initially attached to a protonated amine site of a peptide can subsequently migrate to the site of a disulfide (* orbital, causing disulfide bond cleavage. They also investigated whether the electron attached to a protonated site can migrate to another protonated site or fixed-charge site (Scheme 3).31  Scheme 3. Intramolecular Electron Transfer Mechanism Recent experimental results of the McLuckey research group were cited as evidence that ETD can proceed via an intramolecular electron transfer mechanism.34, 35 The McLuckey group studied ETD of triply charged peptide cations such as the structure depicted in Figure 4. The peptide depicted in Figure 4 is a product of typsin digestion of a protein, somatostatin. An important feature of the peptides they studied was that terminal amine groups of the peptide were fully or partially derivatized by reacting them with a trimethlyammonium butyrate (TMAB) reagent. The TMAB derivatization converted some or all of the amine groups into fixed charge tetramethylammonium sites.34 The peptide cation in Figure 4 does not possess protonated amine groups capable of generating a mobile hydrogen atom after electron transfer. A key finding of the McLuckey group was that the disulfide bond cleaves in the absence of any sites that are known to produce a hydrogen atom upon reduction. The result was considered strong evidence for an alternative mechanism to the hot hydrogen atom transfer model. Another important observation was that the percentage of disulfide bond fragments observed varied among different partially derivatized peptides (Table 1). The Simons and McLuckey groups emphasized the anomalous low percentage of disulfide bond cleavage products and overall cleavage products in a partially derivatized peptide with two fixed charge sites and one protonated site. Intramolecular electron transfer between charged sites was proposed as an intermediate step that could explain the differences. Table 1. ETD reaction products for various peptide cations PeptideTotal Dissociations (%)S-S Dissociations (%)no TMAB8371one TMAB8268two TMABs5236three TMABs6880   Fig. 4. Peptide cation with disulfide bond and three fixed charge terminal groups (top); mass spectrum of ETD products (bottom). The Simons group reported an important theoretical simulation of the ETD process in which they examined competing mechanisms of electron transfer to either a protonated amine Rydberg orbital or to a disulfide (* orbital, when both functional groups are present in the same molecule.32 They predicted that the cross-section for electron transfer to the protonated amine site is an order of magnitude higher than the cross-section for direct transfer to the disulfide bond; however, only a fraction of electrons captured at the charged site will transfer a hydrogen atom to the disulfide, causing it to dissociate. The implication of their study is that direct electron attachment and hot hydrogen atom transfer are competitive process that both occur in peptides and proteins. They chose a small ion, protonated 2-methyldisulfanylethylamine, as a model for their study. They chose methyl anion (CH3-) as their model of an electron transfer agent (A-). The competing processes of electron transfer to the disulfide bond or to the protonated amine group are depicted in Figure 5. The potential energy diagram in Figure 5 depicts the potential energy of this system as a function of the distance (r) between A- and the protonated amine. The potential energy initially decreases as r-1 due to the attraction between positive and negative charges. This potential energy curve (blue) crosses the potential energy curves associated with competing products of electron transfer (green or red). The Simons group calculated the value of r corresponding to curve crossings associated with electron transfer to the disulfide bond (I) or to the -NH3+ group (II), estimating that the former crossing occurs at a distance of 10.75 ; the latter crossing occurs at a distance of 4.31 . Their model supposes a chronology for the approaching CH3-. The ion has an opportunity to transfer an electron to the disulfide bond first. If no transfer occurs, then it has another opportunity to transfer an electron to the protonated amine later.  Fig. 5. Potential Energy Diagram showing Interaction of CH3SSCH2CH2NH3+ and A- The probability of a resonant transfer process at each crossing point was calculated using Landau-Zener theory.36 This theory predicts that the probability of a transition between two potential energy curves at a crossing point depends on the velocity of the approach to the crossing point, the slopes of the potential energy curves, and the strength of coupling between electronic states: Transfer Site Transfer Probability (%) -S-S- 0.0454 -NH3+ 2.67 The probability of electron transfer by either mechanism is low. The probability of electron transfer to -NH3+ is 59 x greater than the probability of transfer to the disulfide. In this study the probability of subsequent intramolecular transfer of a hydrogen atom from the neutralized ammonium radical (II) to the disulfide bond was also factored in and crudely estimated to be 4%. The combined probability of electron transfer to -NH3+ followed by H transfer to the disulfide is approximately 0.1 %. This model of two competing processes suggests that the hot hydrogen atom transfer and Coulomb-assisted direct attachment mechanisms both make significant contributions to ETD. An alternative mechanism of electron capture dissociation has been proposed by Syrstad and Ture ek.37 In their mechanism the captured electron enters into a charge-stabilized electronic state associated with an amide bond. The excited electron in the amide bond acts as a  superbase , which can abstract a proton from a nearby amino acid residue to form an aminoketyl radical. The radical dissociates via N-C( bond cleavage. This mechanism is depicted in Scheme 4.  Scheme 4. Proposed ECD Superbase Mechanism The superbase mechanism is similar to the hot hydrogen transfer and direct electron attachment mechanisms (Schemes 1 and 2). The observable dissociation products are the same. The difference between them involves the sequence in time of electron transfer and proton transfer. Scheme 1 is equivalent to the simultaneous transfer of an electron and a proton; whereas, Scheme 4 depicts electron capture (or transfer) followed later by a proton transfer. Ture ek also proposed a radically different concept about the ECD mechanism by predicting that the rate-limiting step in peptide dissociations may not cleavage of the covalent N-C( bond; rather, the rate-limiting step in some cases was calculated to be breaking of non-covalent bonds in a hydrogen-bonded complex holding the dissociation products together.19 This idea is depicted in Scheme 5. He used density functional theory (DFT) and Mller-Plesset (MP2) ab initio calculations41,42 on small molecules to show that the dissociation energy of a hydrogen bonded complex binding the incipient c- and z- type product ions together can be 67 kJ/mol or greater. The bond dissociation energy (BDE) of a N-C( bond adjacent to an aminoketal radical was calculated to be in the range of 15-30 kJ/mol. The formation of the aminoketal radical at the carbonyl bond site greatly weakens this covalent bond.  EMBED ACD.ChemSketch.20  Scheme 6. Proposed ECD Mechanism with a Stable Hydrogen Bonded Complex The calculations by Ture ek challenged the argument that ECD and ETD are non-ergodic processes.19 Researchers had asserted in early work that ECD must be a non-ergodic process,18 because the recombination energy gained upon electron capture seemed insufficient to cause dissociation, if that energy were partitioned out evenly among the many degrees of freedom in a peptide ion. It would be unlikely for sufficient vibrational excitation energy to accumulate in one covalent bond to cleave it. The more recent ab initio theoretical analysis of bond dissociation and transition-state energies in simple model systems suggested that energy required for N-C( cleavage may be much lower than previously estimated. Dissociation may thus occur rapidly even in fully thermalized charge-reduced ions. More recently, Ture ek et al. have corroborated their theoretical argument about the ergodicity of ECD with experimental results.39 The research of O Connor et al. is a an example of recent experimental work intended to further address questions about the mechanism of ECD raised by Ture ek, Zubarev, and others. This group studied ECD of cyclic peptides and showed that a single electron capture event could produce multiple fragmentations43. They also studied ECD of deuterium labeled peptides and showed that deuterium scrambling occurs.44 They interpreted their results as evidence of a fast (< 1 ps) non-ergodic process coexisting with a much slower (> 1ms) ergodic process.45 Evaluation and Discussion on Findings of the Literature Experiments conducted by the Marshall and McLuckey groups and theoretical studies by the Simons group suggested that the hot hydrogen atom transfer mechanism (Scheme 1) is not consistent with observed dissociation products in EDC and ETD of some peptide cations. Three alternative mechanisms have been proposed to explain processes of ECD and ETD in peptide cations: 1. Coulomb assisted direct electron attachment (Scheme 2) 2. Intramolecular electron transfer (Scheme 3) 3. Proton Transfer to a Superbase (Scheme 4) The overall kinetics of ECD and ETD reactions of peptide cations are not well understood. Questions about the ergodicity of these processes are essentially questions about whether the rate of the dissociation (by any of the mechanisms mentioned above) is faster or slower than the rate of intramolecular vibrational relaxation. Another important open question about the ECD / ETD kinetics is the nature of the rate determining step. Calculations by Ture ek have predicted that the rupture of a hydrogen-bonded intermolecular product complex may be rate determining in ECD. This assessment contradicts the assumption by most other researchers that dissociation of covalent backbone bonds (N-C( or S-S) in a peptide is rate determining. Underlying all of these questions is an assumption that the mechanism (or mechanisms) occurring in ECD and ETD of peptide cations is/are essentially the same, regardless of the whether the peptide cation is reduced by a free electron or by a transferred electron from a donor molecule. There are some comments in the cited literature suggesting that the mechanisms of ECD and ETD might differ in certain cases, but no experimental work has been found directly comparing ECD and ETD dissociation products from the same peptide. The Simons group speculated in their study of protonated and fixed charge cations that because experiments on these peptides were performed using ETD (with the electron transfer agent being nitrobenzene anion) rather than ECD, it is possible that steric hindrance may have precluded the anion reaching the S-S bond site.24 It is thus suggested in the paper that peptide cations might interact differently with free electrons than they do with electron transfer agents of finite molecular size. In their theoretical investigation of competing mechanisms of ETD, the Simons group again mentioned that they chose to use a methyl anion (CH3-) as their model for an electron transfer agent in ab initio calculations. They noted that anions used in real ETD experiments had much larger structures (e.g., of the size of anthracene.) We chose not to use one of these species in our initial investigation because we believe steric factors arising in these larger systems could considerably alter the rates of electron transfer, and we want to focus on the intrinsic rates of such processes.32 Further efforts to define which of the proposed mechanisms of ECD and ETD are dominant in a particular case should perhaps focus more explicitly on the role of the size and structural features of both the electron transfer agent and the peptide cation in guiding the dissociation mechanism. The Coulomb-assisted electron attachment mechanism, for example, requires the cation and anion to approach to a distance where crossing of potential energy surfaces permits the transfer to occur. If either of the ions is too large to approach that distance without steric hindrance, then this reaction pathway will be blocked. Demonstrating that a mechanism switches on or off as a function of molecular size would help to better define the contribution of that mechanism to the dissociation process. Electron affinity is another potentially important feature of electron transfer agents that is absent in ECD. The role of electron affinity could be further investigated to learn how it may alter the efficiency of peptide dissociation mediated by different mechanisms. The electron affinity of the donor molecule affects the amount of internal energy added to the cation when recombination occurs. This recombination energy is used to dissociate covalent bonds. Electron transfer from a molecule with a positive electron affinity imparts less recombination energy to the cation than electron capture of a free electron.20 Research Proposal I propose methods to use the specific structural and electronic properties of electron transfer agents as probes to differentiate among the proposed mechanisms of ECD and ETD. The theoretical work of the Simons group had established that different electron transfer sites on a molecule correspond to different intermolecular distances where resonant electron transfer can occur,32 as depicted in Figure 5. Two sites of electron transfer were available in the singly charged cation that they used as a model. A multiply charged peptide cation would, in general, possess more than two electron transfer sites, but these multiple sites would still be expected to have characteristic intermolecular distances at which the electron transfer may occur. Figure 4 depicts a peptide prepared by the McLuckey group, which was subjected to ETD using the azobenzene anion as an electron transfer agent.34 The average and maximum distances between the disulfide bond and the three charged sites in their peptide cations were calculated from molecular dynamics simulations (Table 2). Table 2. Distances from Charge Sites to the Disulfide in Protonated and Fixed-Charged Peptides Three Protonated SitesThree Fixed ChargesDistance ()AverageMaximumAverage MaximumAla5.0105.416Lys8.8121218Thr6.2191025 The structure of azobenzene is shown in Figure 6. The distance between the two para hydrogens in the molecule is estimated here to be 11.6 from a geometry optimized structure in Hyperchem:  Fig. 6. Geometry Optimized Azobenzene Structure When we compare the distances summarized above to the electron transfer distances of 10.75 for a disulfide (* orbital and 4.31 for a protonated amine, as calculated by Simons, it strongly suggests that some orientations of the peptide cation and azobenzene anion will result in steric hindrance preventing the two ions from reaching a curve-crossing point where electron transfer can occur. Given the molecular sizes and distances between functional groups, it seems likely that steric effects influence the distribution of ETD products in this case. If these peptide cations had been subjected to ECD, the distribution of dissociation products resulting from electron capture in the absence of any steric effects might differ from what was observed. The effect of steric hindrance on ETD has not previously been investigated. I propose that the influence of steric effects in ETD could be investigated both experimentally and in computational simulations by comparing the dissociation products using electron transfer agents with different molecular (or atomic) size. Previous work has demonstrated that a variety of 4, 4- and 3, 3- substituted azobenzene derivatives can be readily synthesized.39, 40 Derivatives could be chosen to increase steric effects in electron transfer.  EMBED ACD.ChemSketch.20  Fig. 7. Example of a 4.4-Disubstituted Azobenzene Derivative The 4,4 dihexylether derivative in Figure 7 is one of many examples of substituted azobenzenes. The distance between terminal methyl groups in this molecule is 25 based on a geometry optimized structure. The radical anion of this substituted azobenzene would be expected in an ETD experiment to generate dissociation products that differ significantly from ECD products due to steric factors. Figure 8 depicts the expected effect of steric hindrance of an anion on electron transfer to three different types of attachment site in a cation: (I) disulfide bond; (II) amide carbonyl double bond; (III) protonated amine. The shaded area represents a distance range where transfers are selectively blocked due to the size of the anion. In this depiction, it is imagined that a hindered anion could be selected to allow only Coulomb stabilized direct attachments to disulfide groups or to amide carbonyl bonds. Attachment to protonated amine groups would be prohibited. Recent experiments have suggested that it is also feasible to investigate ETD using electron transfer agents at the opposite extreme of reagent size. Reactions of peptide cations with neutral cesium vapor produces c- and z- type dissociation products similar to conventional ETD using molecular anions.23 Cesium has a low ionization potential that facilitates transfer of an electron from the neutral atom, converting it into Cs+. Useful information about the supposed steric effects in ETD could be obtained by comparing the ETD products of large molecular anions with monatomic neutrals.  Fig. 8. Depiction of Electron Transfer Directed by Steric Factors Another way in which specific electron transfer agents in ETD differ from the unbound, low-energy electrons used in ECD is that the former have finite, positive electron affinity. Electron affinity represents energy required to remove a bound electron from an anion to affect transfer. The potential energy diagram shown in Figure 9 below depicts electron transfer from an anion with slightly higher electron affinity. As electron affinity increases, the energy level of the transfer products also increases, and the distances associated with curve crossing increase. In the limit of sufficiently high electron affinity the potential energy curve of the ion pair (blue) and an electron transfer product (green) may no longer intersect; thus, no electron transfer will occur to that site.  Figure 9. Electron Transfer Mechanism; Reagent with Higher Electron Affinity Table 3 below summarizes some specific examples of reagents whose anions have been used for ETD.20 Their electron affinities are tabulated versus the percentage of electron transfer dissociation products observed (%ETD) in a typical peptide. Note that the %ETD drops to essentially zero when the electron affinity of the molecule (or atom) exceeds ~60 kcal/mol. The Simons group first suggested that a hypothetical reagent could be selected with electron affinity that selects one electron transfer mechanism over another.32 In the specific case of electron transfer to a small molecule with two types of attachment site (Fig. 5) they predicted that the anion of a hypothetical molecule with an electron affinity of 193 kJ/mol would selectively transfer an electron to the protonated amine site only. Inspection of Table 3 shows that p-dinitrobenzene is one ETD reagent that might be tested with a model peptide cation to verify their prediction. Table 3. Some Precursor Molecules for ETD ReagentEA (kJ/mol)% ETDnorbornadiene23.47.2cis-stilbene43.59.8azobenzene54.848.8fluoranthene60.737.4perylene93.720.9nitrobenzene96.214.7m-dinitrobenzene16026.6o-dinitrobenzene16017.2S2O1817.3p-dinitrobenzene19316.4S32027.0O32034.8NO22198.51,3,5-trinitrobenzene2547.9CO3259<0.01I295<0.01CH3COO324<0.01NO3380<0.01H2PO4441<0.01HSO4458<0.01picric acid473<0.01 Conclusion ECD and ETD are two closely related new dissociation methods that can be used to derive information about the chemical structure of peptides. Several mechanisms have been proposed to explain the products of ECD and ETD. None of the proposals completely succeed. The best interpretation seems to be that more than one competing reaction path is followed. ECD and ETD are typically described in literature as if their mechanisms must be essentially identical, but careful examination of the dissociation products versus structure and electronic properties of different ETD reagents is likely to demonstrate differences. The choice of some alternative ETD reagents, such as sterically hindered molecules or reagents with targeted electron affinity could potentially be used to direct the ETD process to favor one reaction pathway over another. Anions of different ETD reagent molecules or neutral atoms could be used as probes to better understand this process. References Russell, R. B ; Alber, F. ; Aloy, P.; Davis, F. P ; Korkin, D. ; Pichaud, M. ; Topf, M.; Sali, A. Current Opinion in Structural Biology 2004, 14, 313. Minor Jr., D. L. Neuron 2007, 54, 511. Sharon, M.; Robinson, C. V. Annual Review of Biochemistry 2007, 76, 167. Bothner, B.; Siuzdak, G. ChemBioChem, 2004, 5, 258. Nguyen, S.; Fenn, J. B. 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#Yt1`s\mWb`QGڣA=Hxj= .P= nu~D lc Y-X#6Ibc[#75z@o g>D7z{Wo[!͇7q`$etm ]bTI]cG#UG7>0%#CA]SD?L d|x63`7̹lhl?[Fbs U۬1]52M[;O@G:X3T rL"3H{ c;̲>eu65nd +MsڼSjmjRjZj{|DO4loJ{p߫}zv{[xxD<ј/^j,Mj7iyW-bvU*~%u-Ocs^0WNmY3J"CNҥ 4S*m}X3iT5pLcz8oю!h?Z 2v2wP=M䙨^+3d\8YۣDM@ɾ|@7qfrl&|(ޟVA}3v]>ܯh7WO/5?ͦOK ৥Rri!4AKERlWt3 f/ắ#n.'-P'Ka]yXl[Y`RS.y6-c>ʴu{jcqF.(~bo/^~9¹['t`Cpm]rܻfYoG킑>?gh{ 89a0OH1hYRY}_ D)pPɊ[ yɚQN wqH O-91 G;Yض>ǝlt||ʬ_ =U9>bpb+_0{a? +҉wxae!$8(qM.@:eH5yaWa\Q6_ɟ,|“|aˬ[ϩ[. `ϰ ʥ:Ќ(XTPġ*YMk"׎ŗ?6xU:IH룝(zKZ&8Rū";q0vȟQ  w7h1<Հ · \)ʸ?u둯VV_k+^gQ:5[<. ^x;GRkꋗZQnŸp1ŅV}vwS 2.Ŭ+ GyREiJU3r*kg@)WtvF9cє(X|/3D}"Թ 9Wav,8Dd &ww0  # A"H6NcM`@>X$&$@=6NcM`@>XGS^=x] tTf~d&$A +nYkV@nO@;"Pe Rق(lezVPYK{ jtэiiNݍk5|.MfIHfr޹}~"X8OzzzR8l/W QrBXɭB,D< %(ۓi6:'@ TncEvaKP%8|%wnn7NMO.oe+2\w~7A/ׅmH;svg< WH쏧y gRLE9 5>۬2c"'U_1282334185eFQ!=Q!=Ole GPRINTjCompObjHkm  l   --"Systemf !L-.  Arial dww 0wf----$ *(*(,,((*-% *(*(,,((*-$ D**,>,>DD*-% D**,>,>DD* Arialw ww 0wf-2 + k H% - 2 "Uk+ %2 $ (k-1)+ #%-%u  -$  -%  --l$4^`YeUjPrKzGD@>;98889;=? BEI&N.R6V<[A\B^DZ@V;S6O.L&HFC@?>>>?@CFHL~OvSnViZd\b^`-l%4^`YeUjPrKzGD@>;98889;=? BEI&N.R6V<[A\B^DZ@V;S6O.L&HFC@?>>>?@CFHL~OvSnViZd\b^`-l$4d`heljqrvzz~ |x&t.o6k<fAeBdDg@k;n6r.v&y|~~|yv~rvnnkigdebd`-l%4d`heljqrvzz~ |x&t.o6k<fAeBdDg@k;n6r.v&y|~~|yv~rvnnkigdebd` 2 Hqv!Arialf ww 0wf- 2 iO 2 N 2 H 2 CHR  2 sOH 2 /NH 2 LHH 2 CHR  2 rkOH 2 NH 2 HH 2 CHR-%oo%-%y% %? R-%u*%u*-%*+%i)-%qq%-%{%{7%%e*%y---l$4XvS{OJEA>:85322235 79!<*?3C<HDLLPRUWVXXZTVPQMLIDF<B3@*=:98889:=@BFIMPTzVxXv-l%4XvS{OJEA>:85322235 79!<*?3C<HDLLPRUWVXXZTVPQMLIDF<B3@*=:98889:=@BFIMPTzVxXv-l$4^vb{fkptx{} |!y*v3r<nDiLeR`W_X^ZaVeQhLlDp<s3v*x{|}~}|{xvsplheaz_x^v-l%4^vb{fkptx{} |!y*v3r<nDiLeR`W_X^ZaVeQhLlDp<s3v*x{|}~}|{xvsplheaz_x^v - 2 Rkw+--$ 6)\)\+<+<\\66)-% 6)\)\+<+<\\66)-$ ) ) + +     )-% ) ) + +     )2 + ( k-1) H% #---l$4_diqy{xtromlllmoqs vy}%-5;@AC?:5-%|zwtsrrrstwz|}umhca_-l%4_diqy{xtromlllmoqs vy}%-5;@AC?:5-%|zwtsrrrstwz|}umhca_-l$4_diqy %-5;@AC?:5-%}umhca_-l%4_diqy %-5;@AC?:5-%}umhca_ 2 Gv!- 2  O 2  N 2  H 2 E CHR Arial  ww 0wf- 2 tOH-8$- 2 cNH 2 HH 2 CHR  2 qOH 2 NH 2 HH 2 GCHR  2 t3HH-% % -% %$ A %s  Q%v)%)_% (-%%-%%O6%&C%)% . ---l$4 u z ~ y u r n l i g f f f g i k m p )s 2w ;| C K Q V W Y U P K} Cz ;v 2t )q n m l l l m n q t v z } ~ y w u-l%4 u z ~ y u r n l i g f f f g i k m p )s 2w ;| C K Q V W Y U P K} Cz ;v 2t )q n m l l l m n q t v z } ~ y w u-l$4 u z     ) 2 ; C K Q V W Y U P K C ; 2 )    ~ y w u-l%4 u z     ) 2 ; C K Q V W Y U P K C ; 2 )    ~ y w u- 2 Q w+Arialu ww 0wf- 2 A9Arial ww 0wf- 2 l-Arialw ww 0wf- 2  +0- 2 3  HA<9"Systemf &-- -' eFACD/ChemSketchACD.ChemSketch.20ACD.ChemSketch.209q eFACD/ChemSketchACD/ChemSketchACD.ChemSketch.209qOh+'0ObjInfoJOlePres000Ole10Native._1282334045eFQ!=Q!=mb  l   --"Systemt f> !L-.  Arial} dww 0wt f>----$ *(*(,,((*-% *(*(,,((*-$ D**,>,>DD*-% D**,>,>DD* Arial dww 0wt f>-2 + k H% - 2 "Uk+ %2 $ (k-1)+ #%-%u  -$  -%  --l$4^`YeUjPrKzGD@>;98889;=? BEI&N.R6V<[A\B^DZ@V;S6O.L&HFC@?>>>?@CFHL~OvSnViZd\b^`-l%4^`YeUjPrKzGD@>;98889;=? BEI&N.R6V<[A\B^DZ@V;S6O.L&HFC@?>>>?@CFHL~OvSnViZd\b^`-l$4d`heljqrvzz~ |x&t.o6k<fAeBdDg@k;n6r.v&y|~~|yv~rvnnkigdebd`-l%4d`heljqrvzz~ |x&t.o6k<fAeBdDg@k;n6r.v&y|~~|yv~rvnnkigdebd` 2 Hqv!Ariall ww 0wt f>- 2 iO 2 N 2 H 2 CHR  2 sOH 2 /NH 2 LHH 2 CHR  2 rkOH 2 NH 2 HH 2 CHR-%oo%-%y% %? R-%u*%u*-%*+%i)-%qq%-%{%{7%%e*%y---l$4XvS{OJEA>:85322235 79!<*?3C<HDLLPRUWVXXZTVPQMLIDF<B3@*=:98889:=@BFIMPTzVxXv-l%4XvS{OJEA>:85322235 79!<*?3C<HDLLPRUWVXXZTVPQMLIDF<B3@*=:98889:=@BFIMPTzVxXv-l$4^vb{fkptx{} |!y*v3r<nDiLeR`W_X^ZaVeQhLlDp<s3v*x{|}~}|{xvsplheaz_x^v-l%4^vb{fkptx{} |!y*v3r<nDiLeR`W_X^ZaVeQhLlDp<s3v*x{|}~}|{xvsplheaz_x^v - 2 Rkw+--$ 6)\)\+<+<\\66)-% 6)\)\+<+<\\66)-$ ) ) + +     )-% ) ) + +     )2 + ( k-1) H% #---l$4_diqy{xtromlllmoqs vy}%-5;@AC?:5-%|zwtsrrrstwz|}umhca_-l%4_diqy{xtromlllmoqs vy}%-5;@AC?:5-%|zwtsrrrstwz|}umhca_-l$4_diqy %-5;@AC?:5-%}umhca_-l%4_diqy %-5;@AC?:5-%}umhca_ 2 Gv!- 2  O 2  N 2  H 2 E CHR Arial uww 0wt f>- 2 tOH-8$- 2 cNH 2 HH 2 CHR  2 qOH 2 NH 2 HH 2 GCHR  2 t3HH-% % -% %$ A %s  Q%v)%)_% (-%%-%%O6%&C%)% . ---l$4 u z ~ y u r n l i g f f f g i k m p )s 2w ;| C K Q V W Y U P K} Cz ;v 2t )q n m l l l m n q t v z } ~ y w u-l%4 u z ~ y u r n l i g f f f g i k m p )s 2w ;| C K Q V W Y U P K} Cz ;v 2t )q n m l l l m n q t v z } ~ y w u-l$4 u z     ) 2 ; C K Q V W Y U P K C ; 2 )    ~ y w u-l%4 u z     ) 2 ; C K Q V W Y U P K C ; 2 )    ~ y w u- 2 Q w+Arial ww 0wt f>- 2 A9Arial} ww 0wt f>- 2 l-Arial fww 0wt f>- 2  +0- 2 3  HA<9"System>t f> &-- -'*'''?,Arial,(Arial,(Arial,2Arial, , vArial,Arial,Arial,Arial,Arial,Arial,Arial,,Arial,Arial,Arial,Arial,(Arial,Arial,Arial,+Arial,Arial,Arial,Arial,Arial,Arial,Arial,-Arial,Arial,Arial,Arial,%Arial,Arial,Arial,7^  4 AjCDjCDD ADBlPD0fCPD0CPD0CPD0fCPD0fCPD0fCPD0fCAFT+ k Hi+DPC؋DݜC۳DC+DPC؋DPC+DPC؋DPCAFT[k+mAERC"LEɝCFE؉CAERC"LERCAERC"LERCAFT(k-1)+"(DzCDzC 4.B!CC!CCD.BDBhCDCC"DC" DCDCCDCCDCCDCAFT&v)4x? 6eDC)4x? 6eD@C)4x? zDhC4x? kD@CCHR{\rtf1\ansi\ansicpg1252\deff0\deflang1033{\fonttbl{\f0\fnil\fcharset0 Arial;}{\f1\fnil Arial;}} \viewkind4\uc1\pard\fs20 CHR\sub\f1\par } )J? DiD)4x? vDiD)J? vDC)4x? FDзC4x? W4DCCHR{\rtf1\ansi\ansicpg1252\deff0\deflang1033{\fonttbl{\f0\fnil\fcharset0 Arial;}{\f1\fnil Arial;}} \viewkind4\uc1\pard\fs20 CHR\sub\f1\par } )4x? `CC)4x? `C@C)4x? pjChC)J? [BfC4x? LC@CCHR{\rtf1\ansi\ansicpg1252\deff0\deflang1033{\fonttbl{\f0\fnil\fcharset0 Arial;}{\f1\fnil Arial;}} \viewkind4\uc1\pard\fs20 CHR\sub\f1\par } 4x? l4x? 4x?  )4x? [4x? 54x? G4x? 4x? ^4x? 4x? 74x? +4x? 4x?  4eSD!C4D!C4DiDeSDiDBh(D"AD(AD"D(D"a D(D"AD(AD"AD(D"AD(AD"ADAFT+w 44DiC@EiC@ED4DDBq(3.E0C(FE0fC(:E0&C(3.E0C(FE0C(3.E0C(FE0CAFT + ( k-1) H 4D衏C40D衏C40DDDDBh(!DDC(D"D(D" D(!DDC(DDC(!DDC(DDCAFT&v)4x? E/C)4x? E@BC)4x? !EhKC4x? &E@BCCHR{\rtf1\ansi\ansicpg1252\deff0\deflang1033{\fonttbl{\f0\fnil\fcharset0 Arial;}{\f1\fnil Arial;}} \viewkind4\uc1\pard\fs20 CHR\sub\f1\par } )J? R2/E)D)? E)D)? E@C)4x? E7C4x? UE@CCHR{\rtf1\ansi\ansicpg1252\deff0\deflang1033{\fonttbl{\f0\fnil\fcharset0 Arial;}{\f1\fnil Arial;}} \viewkind4\uc1\pard\fs20 CHR\sub\f1\par } )4x?  [D/C)4x?  [D@BC)4x? nDhKC)J? l^DC4x? +D@BCCHR{\rtf1\ansi\ansicpg1252\deff0\deflang1033{\fonttbl{\f0\fnil\fcharset0 Arial;}{\f1\fnil Arial;}} \viewkind4\uc1\pard\fs20 CHR\sub\f1\par } )4x? ED4x?  k 4x?   4x? @ ] 4x?   4x? :6:4x? :{4x? 4x? ]4x?  4x? k4x? B_4x? :4x?  J 4x?  4tE衚C8-E衚C8-E)DtE)DBh+E"D`.E"AD-E"! D+E"D`.E"D+E"D`.E"DAFT+wsDCDCDCDCDCDCDCAFTA-uAECOECHECAECOECAECOECAFT+ HAOle KPRINT<+CompObjLhObjInfoNL      !"#$%&'()*+,-/0123456789:;<=>?@ABCDEFGHIJMOPQRSTUVWXYZ[\]^_`abcdefghijklmnopqrstuvwxyz{|}~i!  l g  --"Systemf !L-.  Arial{ dww 0wf----$ *(*(,,((*-% *(*(,,((*-$ D**,>,>DD*-% D**,>,>DD* Arial ww 0wf-2 + k H% - 2 "Uk+ %2 $ (k-1)+ #%-%u  -$  -%   2 ]m+5% !Arial ߸ww 0wf- 2 `++, -2  + n H%#- 2 ^ n+#%@%            % * D% /7?GOW[`eilnoppoymsjqhkdg`c[`U^O]I\C\=]7_1b+d(e&%e&BE--l$4^`YeUjPrKzGD@>;98889;=? BEI&N.R6V<[A\B^DZ@V;S6O.L&HFC@?>>>?@CFHL~OvSnViZd\b^`-l%4^`YeUjPrKzGD@>;98889;=? BEI&N.R6V<[A\B^DZ@V;S6O.L&HFC@?>>>?@CFHL~OvSnViZd\b^`-l$4d`heljqrvzz~ |x&t.o6k<fAeBdDg@k;n6r.v&y|~~|yv~rvnnkigdebd`-l%4d`heljqrvzz~ |x&t.o6k<fAeBdDg@k;n6r.v&y|~~|yv~rvnnkigdebd` 2 Hqv!Arials ww 0wf- 2 iO 2 N 2 H 2 CHR  2 sOH 2 /NH 2 LHH 2 CHR  2 rkOH 2 NH 2 HH 2 CHR-%oo%-%y% %? R-%u*%u*-%*+%i)-%qq%-%{%{7%%e*%y---l$4XvS{OJEA>:85322235 79!<*?3C<HDLLPRUWVXXZTVPQMLIDF<B3@*=:98889:=@BFIMPTzVxXv-l%4XvS{OJEA>:85322235 79!<*?3C<HDLLPRUWVXXZTVPQMLIDF<B3@*=:98889:=@BFIMPTzVxXv-l$4^vb{fkptx{} |!y*v3r<nDiLeR`W_X^ZaVeQhLlDp<s3v*x{|}~}|{xvsplheaz_x^v-l%4^vb{fkptx{} |!y*v3r<nDiLeR`W_X^ZaVeQhLlDp<s3v*x{|}~}|{xvsplheaz_x^v - 2 Rkw+--$ 6)\)\+<+<\\66)-% 6)\)\+<+<\\66)-$ x )R )R +r +r R R x x )-% x )R )R +r +r R R x x )2 + k H% ---l$4_diqy{xtromlllmoqs vy}%-5;@AC?:5-%|zwtsrrrstwz|}umhca_-l%4_diqy{xtromlllmoqs vy}%-5;@AC?:5-%|zwtsrrrstwz|}umhca_-l$4_diqy %-5;@AC?:5-%}umhca_-l%4_diqy %-5;@AC?:5-%}umhca_ 2 Gv!- 2  O 2  N 2  H 2 E CHR Arial ww 0wf- 2 tOH-8$- 2 cNH 2 HH 2 CHR  2 qOH 2 NH 2 HH 2 GCHR  2 t3HH-% % -% %$ A %s  Q%v)%)_% (-%%-%%O6%&C%)% . ---l$4 u z ~ y u r n l i g f f f g i k m p )s 2w ;| C K Q V W Y U P K} Cz ;v 2t )q n m l l l m n q t v z } ~ y w u-l%4 u z ~ y u r n l i g f f f g i k m p )s 2w ;| C K Q V W Y U P K} Cz ;v 2t )q n m l l l m n q t v z } ~ y w u-l$4 u z     ) 2 ; C K Q V W Y U P K C ; 2 )    ~ y w u-l%4 u z     ) 2 ; C K Q V W Y U P K C ; 2 )    ~ y w u- 2 Q w+--$ 0lVlVn6n6VV00l-% 0lVlVn6n6VV00l-$ llnnl-% llnnl2 #+ m H%5---l$4~yurnligfffg,i9kCmMpVs_wh|px~}x}pzhv_tVqJn=m/l"llmnqtvz}-l%4~yurnligfffg,i9kCmMpVs_wh|px~}x}pzhv_tVqJn=m/l"llmnqtvz}-l$4,9CMV_hpx~}xph_VJ=/"-l%4,9CMV_hpx~}xph_VJ=/" 2 v!--$ p@p@r r @@p-% p@p@r r @@p-$ u pO pO ro ro O O u u p-% u pO pO ro ro O O u u p- 2 % O 2 >z N 2 > H 2  CHR  2 ICH 2 IHH-z Arial dww 0wf-2 gRH-%+ + %%? ? %-%5 %v J% @ /% :_ %5 %M%K|---l$4      -:DNW`i q y      ~ y q i`WK>0#       -l%4      -:DNW`i q y      ~ y q i`WK>0#       -l$4  " ' , 0 4 7 9 < > ? ? ? > -= :; D8 N5 W2 `. i* q% y!     ! ~$ y( q, i/ `2 W4 K7 >8 09 #: 9 8 7 4 2 / , ( $ !    -l%4  " ' , 0 4 7 9 < > ? ? ? > -= :; D8 N5 W2 `. i* q% y!     ! ~$ y( q, i/ `2 W4 K7 >8 09 #: 9 8 7 4 2 / , ( $ !    Arial{ ww 0wf- 2 ' w+- 2  O- 2 $]N 2 $zH 2 32  2 O 2 EN 2 E H 2 ACHR-%""l%l-%lYF-%,%,-%,Q%,Iy% G=6%Al-%~~B--$~Bi~-%~Bi~ Arial ww 0wf- 2 A9Arials ww 0wf- 2 l-Arial ww 0wf- 2 +0- 2  A9"Systemf &-- -'OlePres000v+Ole10Native"1TableNESummaryInformation( Oi!4+  l g  --"System{f !-.  Arials ww 0w{f----$ *(*(,,((*-% *(*(,,((*-$ D**,>,>DD*-% D**,>,>DD* Arial ww 0w{f-2 + k H% - 2 "Uk+ %2 $ (k-1)+ #%-%u  -$  -%   2 ]m+5% !Arial ww 0w{f- 2 `++, -2  + n H%#- 2 ^ n+#%@%            % * D% /7?GOW[`eilnoppoymsjqhkdg`c[`U^O]I\C\=]7_1b+d(e&%e&BE--l$4^`YeUjPrKzGD@>;98889;=? BEI&N.R6V<[A\B^DZ@V;S6O.L&HFC@?>>>?@CFHL~OvSnViZd\b^`-l%4^`YeUjPrKzGD@>;98889;=? BEI&N.R6V<[A\B^DZ@V;S6O.L&HFC@?>>>?@CFHL~OvSnViZd\b^`-l$4d`heljqrvzz~ |x&t.o6k<fAeBdDg@k;n6r.v&y|~~|yv~rvnnkigdebd`-l%4d`heljqrvzz~ |x&t.o6k<fAeBdDg@k;n6r.v&y|~~|yv~rvnnkigdebd` 2 Hqv!Arial ww 0w{f- 2 iO 2 N 2 H 2 CHR  2 sOH 2 /NH 2 LHH 2 CHR  2 rkOH 2 NH 2 HH 2 CHR-%oo%-%y% %? R-%u*%u*-%*+%i)-%qq%-%{%{7%%e*%y---l$4XvS{OJEA>:85322235 79!<*?3C<HDLLPRUWVXXZTVPQMLIDF<B3@*=:98889:=@BFIMPTzVxXv-l%4XvS{OJEA>:85322235 79!<*?3C<HDLLPRUWVXXZTVPQMLIDF<B3@*=:98889:=@BFIMPTzVxXv-l$4^vb{fkptx{} |!y*v3r<nDiLeR`W_X^ZaVeQhLlDp<s3v*x{|}~}|{xvsplheaz_x^v-l%4^vb{fkptx{} |!y*v3r<nDiLeR`W_X^ZaVeQhLlDp<s3v*x{|}~}|{xvsplheaz_x^v - 2 Rkw+--$ 6)\)\+<+<\\66)-% 6)\)\+<+<\\66)-$ x )R )R +r +r R R x x )-% x )R )R +r +r R R x x )2 + k H% ---l$4_diqy{xtromlllmoqs vy}%-5;@AC?:5-%|zwtsrrrstwz|}umhca_-l%4_diqy{xtromlllmoqs vy}%-5;@AC?:5-%|zwtsrrrstwz|}umhca_-l$4_diqy %-5;@AC?:5-%}umhca_-l%4_diqy %-5;@AC?:5-%}umhca_ 2 Gv!- 2  O 2  N 2  H 2 E CHR Arialz ww 0w{f- 2 tOH-8$- 2 cNH 2 HH 2 CHR  2 qOH 2 NH 2 HH 2 GCHR  2 t3HH-% % -% %$ A %s  Q%v)%)_% (-%%-%%O6%&C%)% . ---l$4 u z ~ y u r n l i g f f f g i k m p )s 2w ;| C K Q V W Y U P K} Cz ;v 2t )q n m l l l m n q t v z } ~ y w u-l%4 u z ~ y u r n l i g f f f g i k m p )s 2w ;| C K Q V W Y U P K} Cz ;v 2t )q n m l l l m n q t v z } ~ y w u-l$4 u z     ) 2 ; C K Q V W Y U P K C ; 2 )    ~ y w u-l%4 u z     ) 2 ; C K Q V W Y U P K C ; 2 )    ~ y w u- 2 Q w+--$ 0lVlVn6n6VV00l-% 0lVlVn6n6VV00l-$ llnnl-% llnnl2 #+ m H%5---l$4~yurnligfffg,i9kCmMpVs_wh|px~}x}pzhv_tVqJn=m/l"llmnqtvz}-l%4~yurnligfffg,i9kCmMpVs_wh|px~}x}pzhv_tVqJn=m/l"llmnqtvz}-l$4,9CMV_hpx~}xph_VJ=/"-l%4,9CMV_hpx~}xph_VJ=/" 2 v!--$ p@p@r r @@p-% p@p@r r @@p-$ u pO pO ro ro O O u u p-% u pO pO ro ro O O u u p- 2 % O 2 >z N 2 > H 2  CHR  2 ICH 2 IHH-z Arial zww 0w{f-2 gRH-%+ + %%? ? %-%5 %v J% @ /% :_ %5 %M%K|---l$4      -:DNW`i q y      ~ y q i`WK>0#       -l%4      -:DNW`i q y      ~ y q i`WK>0#       -l$4  " ' , 0 4 7 9 < > ? ? ? > -= :; D8 N5 W2 `. i* q% y!     ! ~$ y( q, i/ `2 W4 K7 >8 09 #: 9 8 7 4 2 / , ( $ !    -l%4  " ' , 0 4 7 9 < > ? ? ? > -= :; D8 N5 W2 `. i* q% y!     ! ~$ y( q, i/ `2 W4 K7 >8 09 #: 9 8 7 4 2 / , ( $ !    Arials ww 0w{f- 2 ' w+- 2  O- 2 $]N 2 $zH 2 32  2 O 2 EN 2 E H 2 ACHR-%""l%l-%lYF-%,%,-%,Q%,Iy% G=6%Al-%~~B--$~Bi~-%~Bi~ Arial ww 0w{f- 2 A9Arial ww 0w{f- 2 l-Arialz ww 0w{f- 2 +0- 2  A9"System{f &-- -'NANI"''"'?,#Arial,$Arial,(Arial,(Arial,2Arial, ,  , KvArial,Arial,Arial,Arial,Arial,Arial,Arial,,Arial,Arial,Arial,Arial,(Arial,Arial,Arial,+Arial,Arial,Arial,Arial,(Arial,Arial,Arial,+Arial,Arial,Arial,Arial,(Arial,Arial,Arial,;,Arial,Arial,Arial,Arial,Arial,Arial,Arial,-Arial,Arial,Arial,Arial,%Arial,Arial,Arial,7^  4(C@DYD@DYDD(CDBl PFDٴDPDDPDiDPFDٴDPDٴDPFDٴDPDٴDAFT+ k Hi ׋D|DD|7D;D|D׋D|DD|D׋D|DD|DAFT[k+m BEvRDMEvrD:HEvDBEvRDMEvRDBEvRDMEvRDAFT(k-1)+" DDEDD i lDvrDEvDluDvDlDvrDEvrDlDvrDEvrDAFTym+p ??hEE8EHEEEhEE8EEhEE8EEAFT-+l 4EYD=E<E8EE4EYD=EYD4EYD=EYDAFT+ n Hi rCEvDrLEvDGEv"DrCEvDrLEvDrCEvDrLEvDAFTn+UE;uDbK1E߸D_$AqlA_E/D_AlAq}ZA gAZE'qD\kaAuQ> E/D_AlA_AlA:EΐDl_Al_A}E?bD_l_l1E߸DlA_lA_cEDk@"_A{ExcDZAqa#NAzEDNqaNqaEDqaA#N>hBE%DA>SN 6gA] EaDNAqaANAqaA{ExcDqa#NAqa#NAzEDNqaNqaEDqaA#NqaA#N 4J^CzDf DzDf DtDJ^CtDBh PDDPDDP DpDPDDPDDPDDPDDAFT&v)4x? 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