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1.
Aleksey Vorobyev Hisham Ben Hamidane Yury O. Tsybin 《Journal of the American Society for Mass Spectrometry》2009,20(12):2273-2283
We present mechanistic studies aimed at improving the understanding of the product ion formation rules in electron capture dissociation (ECD) of peptides and proteins in Fourier transform ion cyclotron resonance mass spectrometry. In particular, we attempted to quantify the recently reported general correlation of ECD product ion abundance (PIA) with amino acid hydrophobicity. The results obtained on a series of model H-RAAAAXAAAAK-OH peptides confirm a direct correlation of ECD PIA with X amino acid hydrophobicity and polarity. The correlation factor (R) exceeds 0.9 for 12 amino acids (Ile, Val, His, Asn, Asp, Glu, Gln, Ser, Thr, Gly, Cys, and Ala). The deviation of ECD PIA for seven outliers (Pro is not taken into consideration) is explained by their specific radical stabilization properties (Phe, Trp, Tyr, Met, and Leu) and amino acid basicity (Lys, Arg). Phosphorylation of Ser, Thr, and Tyr decreases the efficiency of ECD around phosphorylated residues, as expected. The systematic arrangement of amino acids reported here indicates a possible route toward development of a predictive model for quantitative electron capture/transfer dissociation tandem mass spectrometry, with possible applications in proteomics. 相似文献
2.
3.
Thi Nga Le Jean Christophe Poully Frédéric Lecomte Nicolas Nieuwjaer Bruno Manil Charles Desfrançois Fabien Chirot Jerome Lemoine Philippe Dugourd Guillaume van der Rest Gilles Grégoire 《Journal of the American Society for Mass Spectrometry》2013,24(12):1937-1949
The gas-phase structures of doubly and triply protonated Amyloid-β12-28 peptides have been investigated through the combination of ion mobility (IM), electron capture dissociation (ECD) mass spectrometry, and infrared multi-photon dissociation (IRMPD) spectroscopy together with theoretical modeling. Replica-exchange molecular dynamics simulations were conducted to explore the conformational space of these protonated peptides, from which several classes of structures were found. Among the low-lying conformers, those with predicted diffusion cross-sections consistent with the ion mobility experiment were further selected and their IR spectra simulated using a hybrid quantum mechanical/semiempirical method at the ONIOM DFT/B3LYP/6-31 g(d)/AM1 level. In ECD mass spectrometry, the c/z product ion abundance (PIA) has been analyzed for the two charge states and revealed drastic differences. For the doubly protonated species, N – Cα bond cleavage occurs only on the N and C terminal parts, while a periodic distribution of PIA is clearly observed for the triply charged peptides. These PIA distributions have been rationalized by comparison with the inverse of the distances from the protonated sites to the carbonyl oxygens for the conformations suggested from IR and IM experiments. Structural assignment for the amyloid peptide is then made possible by the combination of these three experimental techniques that provide complementary information on the possible secondary structure adopted by peptides. Although globular conformations are favored for the doubly protonated peptide, incrementing the charge state leads to a conformational transition towards extended structures with 310- and α-helix motifs. 相似文献
4.
Xiaojuan Li Cheng Lin Liang Han Catherine E. Costello Peter B. O’Connor 《Journal of the American Society for Mass Spectrometry》2010,21(4):646-656
Secondary fragmentations of three synthetic peptides (human αA crystallin peptide 1-11, the deamidated form of human βB2 crystallin peptide 4-14, and amyloid β peptide 25-35) were studied in both electron capture dissociation (ECD) and electron-transfer dissociation (ETD) mode. In
ECD, in addition to c and z· ion formations, charge remote fragmentations (CRF) of z· ions were abundant, resulting in internal
fragment formation or partial/entire side-chain losses from amino acids, sometimes several residues away from the backbone
cleavage site, and to some extent multiple side-chain losses. The internal fragments were observed in peptides with basic
residues located in the middle of the sequences, which was different from most tryptic peptides with basic residues located
at the C-terminus. These secondary cleavages were initiated by hydrogen abstraction at the α-, β-, or γ-position of the amino acid side chain. In comparison, ETD generates fewer CRF fragments than ECD. This secondary cleavage
study will facilitate ECD/ETD spectra interpretation, and help de novo sequencing and database searching. 相似文献
5.
Takashi Nishikazea Mitsuo Takayama 《Journal of the American Society for Mass Spectrometry》2010,21(12):1979-1988
Although conventional N-Cα bond cleavage in electron capture dissociation (ECD) of multiply-charged peptides generates a complementary
c′ and z′ fragment pair, the N-Cα cleavage followed by hydrogen transfer from c′ to z′ fragments produces other fragments,
namely c′ and z′. In this study, the influence of charge state and amino acid composition on hydrogen transfer in ECD is described
using sets of peptides. Hydrogen transferred ionic species such as c′ and z′ were observed in ECD spectra of doubly-protonated
peptides, while the triply-protonated form did not demonstrate hydrogen transfer. The extent of hydrogen transfer in ECD of
doubly-protonated peptides was dependent on constituent amino acids. The ECD of doubly-protonated peptides possessing numerous
basic sites showed extensive hydrogen transfer compared with ECD of less basic peptides. The extent of hydrogen transfer is
discussed from the viewpoints of the structure of peptide ions, the possibility of internal hydrogen bonding and intermediate
lifetime of complex [c′+z′]. 相似文献
6.
Fagerquist CK Hudgins RR Emmett MR Håkansson K Marshall AG 《Journal of the American Society for Mass Spectrometry》2003,14(4):302-310
Desfuroylceftiofur (DFC) is a bioactive beta-lactam antibiotic metabolite that has a free thiol group. Previous experiments have shown release of DFC from plasma extracts after addition of a disulfide reducing agent, suggesting that DFC may be bound to plasma and tissue proteins through disulfide bonds. We have reacted DFC with [Arg(8)]-vasopressin (which has one disulfide bond) and bovine insulin (which has three disulfide bonds) and analyzed the reaction products by use of electron capture dissociation Fourier transform ion cyclotron resonance mass spectrometry (ECD FT-ICR MS), which has previously shown preferential cleavage of disulfide bonds. We observe cleavage of DFC from vasopressin and insulin during ECD, suggesting that DFC is indeed bound to peptides and proteins through disulfide bonds. Specifically, we observed dissociative loss of one, as well as two, DFC species during ECD of [vasopressin + 2(DFC-H) + 2H](2+) from a single electron capture event. Loss of two DFCs could arise from either consecutive or simultaneous loss, but in any case implies a gas phase disulfide exchange step. ECD of [insulin + DFC + 4H](4+) shows preferential dissociative loss of DFC. Combined with HPLC, ECD FT-ICR-MS may be an efficient screening method for detection of drug-biomolecule binding. 相似文献
7.
Rand KD Adams CM Zubarev RA Jørgensen TJ 《Journal of the American Chemical Society》2008,130(4):1341-1349
Hydrogen (1H/2H) exchange combined with mass spectrometry (HX-MS) has become a recognized method for the analysis of protein structural dynamics. Presently, the incorporated deuterons are typically localized by enzymatic cleavage of the labeled proteins and single residue resolution is normally only obtained for a few residues. Determination of site-specific deuterium levels by gas-phase fragmentation in tandem mass spectrometers would greatly increase the applicability of the HX-MS method. The biggest obstacle in achieving this goal is the intramolecular hydrogen migration (i.e., hydrogen scrambling) that occurs during vibrational excitation of gas-phase ions. Unlike traditional collisional ion activation, electron capture dissociation (ECD) is not associated with substantial vibrational excitation. We investigated the extent of intramolecular backbone amide hydrogen (1H/2H) migration upon ECD using peptides with a unique selective deuterium incorporation. Our results show that only limited amide hydrogen migration occurs upon ECD, provided that vibrational excitation prior to the electron capture event is minimized. Peptide ions that are excessively vibrationally excited in the electrospray ion source by, e.g., high declustering potentials or during precursor ion selection (via sideband excitation) in the external linear quadrupole ion trap undergo nearly complete hydrogen (1H/2H) scrambling. Similarly, collision-induced dissociation (CID) in the external linear quadrupole ion trap results in complete or extensive hydrogen (1H/2H) scrambling. This precludes the use of CID as a method to obtain site-specific information from proteins that are labeled in solution-phase 1H/2H exchange experiments. In contrast, the deuteration levels of the c- and z-fragment ions generated from ECD closely mimic the known solution deuteration pattern of the selectively labeled peptides. This excellent correlation between the results obtained from gas phase and solution suggests that ECD holds great promise as a general method to obtain single residue resolution in proteins from solution 1H/2H exchange experiments. 相似文献
8.
Pan J Han J Borchers CH Konermann L 《Journal of the American Chemical Society》2008,130(35):11574-11575
Mass spectrometry (MS) methods involving gas-phase fragmentation hold considerable promise for analyzing regioselective deuteration patterns of proteins following solution-phase amide hydrogen exchange (HX). However, the general viability of such an approach is questionable due to the possible occurrence of intramolecular hydrogen migration ("scrambling"), which tends to randomize or distort the spatial isotope distribution. Rand et al. (J. Am. Chem. Soc. 2008, 130, 1341-1349) have recently reported the application of electron capture dissociation (ECD) for measuring deuteration patterns of short peptides with very little scrambling by FT-MS. The current work shows that even much larger systems such as the 76-residue protein ubiquitin can be successfully analyzed by ECD following solution-phase HX. The resulting c and z. ion deuteration levels are in remarkable agreement with previous NMR data, demonstrating that the extent of scrambling and/or other gas-phase artifacts is negligible. These results open the door to future experiments on the folding, structure, and dynamics of proteins by HX/ECD-FT-MS. 相似文献
9.
Guan Z 《Journal of the American Society for Mass Spectrometry》2002,13(12):1443-1447
Electron capture dissociation (ECD) has been demonstrated to be an effective fragmentation technique for characterizing the site and structure of the fatty acid modification in ghrelin, a 28-residue growth-hormone-releasing peptide that has an unusual ester-linked n-octanoyl (C8:0) modification at Ser-3. ECD cleaves 21 of 23 possible backbone amine bonds, with the product ions (c and z· ions) covering a greater amino acid sequence than those obtained by collisionally activated dissociation (CAD). Consistent with the ECD nonergodic mechanism, the ester-linked octanoyl group is retained on all backbone cleavage product ions, allowing for direct localization of this labile modification. In addition, ECD also induces the ester bond cleavage to cause the loss of octanoic acid from the ghrelin molecular ion; the elimination process is initiated by the capture of an electron at the protonated ester group, which is followed by the radical-site-initiated reaction known as -cleavage. The chemical composition of the attached fatty acid can be directly obtained from the accurate Fourier transform ion cyclotron resonance (FTICR) mass measurement of the ester bond cleavage product ions. 相似文献
10.
Andrew W. Jones Victor A. Mikhailov Jesus Iniesta Helen J. Cooper 《Journal of the American Society for Mass Spectrometry》2010,21(2):268-277
In vivo protein nitration is associated with many disease conditions that involve oxidative stress and inflammatory response.
The modification involves addition of a nitro group at the position ortho to the phenol group of tyrosine to give 3-nitrotyrosine. To understand the mechanisms and consequences of protein nitration,
it is necessary to develop methods for identification of nitrotyrosine-containing proteins and localization of the sites of
modification. Here, we have investigated the electron capture dissociation (ECD) and collision-induced dissociation (CID)
behavior of 3-nitrotyrosine-containing peptides. The presence of nitration did not affect the CID behavior of the peptides.
For the doubly-charged peptides, addition of nitration severely inhibited the production of ECD sequence fragments. However,
ECD of the triply-charged nitrated peptides resulted in some singly-charged sequence fragments. ECD of the nitrated peptides
is characterized by multiple losses of small neutral species including hydroxyl radicals, water and ammonia. The origin of
the neutral losses has been investigated by use of activated ion (AI) ECD. Loss of ammonia appears to be the result of non-covalent
interactions between the nitro group and protonated lysine side-chains. 相似文献
11.
Hisham Ben Hamidane Diego Chiappe Ralf Hartmer Aleksey Vorobyev Marc Moniatte Yury O. Tsybin 《Journal of the American Society for Mass Spectrometry》2009,20(4):567-575
We decoupled electron-transfer dissociation (ETD) and collision-induced dissociation of charge-reduced species (CRCID) events
to probe the lifetimes of intermediate radical species in ETD-based ion trap tandem mass spectrometry of peptides. Short-lived
intermediates formed upon electron transfer require less energy for product ion formation and appear in regular ETD mass spectra,
whereas long-lived intermediates require additional vibrational energy and yield product ions as a function of CRCID amplitude.
The observed dependencies complement the results obtained by double-resonance electron-capture dissociation (ECD) Fourier
transform ion cyclotron resonance mass spectrometry (FT-ICR MS) and ECD in a cryogenic ICR trap. Compared with ECD FT-ICR
MS, ion trap MS offers lower precursor ion internal energy conditions, leading to more abundant charge-reduced radical intermediates
and larger variation of product ion abundance as a function of vibrational post-activation amplitude. In many cases decoupled
CRCID after ETD exhibits abundant radical c-type and even-electron z-type ions, in striking contrast to predominantly even-electron c-type and radical z-type ions in ECD FT-ICR MS and especially activated ion-ECD, thus providing a new insight into the fundamentals of ECD/ETD. 相似文献
12.
McLafferty FW Horn DM Breuker K Ge Y Lewis MA Cerda B Zubarev RA Carpenter BK 《Journal of the American Society for Mass Spectrometry》2001,12(3):245-249
Fourier-transform ion cyclotron resonance instrumentation is uniquely applicable to an unusual new ion chemistry, electron capture dissociation (ECD). This causes nonergodic dissociation of far larger molecules (42 kDa) than previously observed (<1 kDa), with the resulting unimolecular ion chemistry also unique because it involves radical site reactions for similarly larger ions. ECD is highly complementary to the well known energetic methods for multiply charged ion dissociation, providing much more extensive protein sequence information, including the direct identification of N- versus C-terminal fragment ions. Because ECD only excites the molecule near the cleavage site, accompanying rearrangements are minimized. Counterintuitively, cleavage of backbone covalent bonds of protein ions is favored over that of noncovalent bonds; larger (>10 kDa) ions give far more extensive ECD if they are first thermally activated. This high specificity for covalent bond cleavage also makes ECD promising for studying the secondary and tertiary structure of gaseous protein ions caused by noncovalent bonding. 相似文献
13.
Probing the mechanism of electron capture dissociation on variously modified model peptide polycations has resulted in discovering
many ways to prevent or reduce $ {\text{N}} - {{\text{C}}_α } $ {\text{N}} - {{\text{C}}_α } bond fragmentation. Here we report on a rare finding of how to increase the backbone bond dissociation rate. In a number
of model peptides, amide-to-ester backbone bond substitution increased the frequency of $ {\text{O}} - {{\text{C}}_α } $ {\text{O}} - {{\text{C}}_α } bond cleavage (an analogue of $ {\text{N}} - {{\text{C}}_α } $ {\text{N}} - {{\text{C}}_α } bonds in normal peptides) by several times, at the expense of reduced frequency of cleavages of the neighboring $ {\text{N}} - {{\text{C}}_α } $ {\text{N}} - {{\text{C}}_α } bonds. In contrast, the ester linkage was only marginally broken in collisional dissociation. These results further highlight
the complementarity of the reaction mechanisms in electron capture dissociation (ECD) and collision-activated dissociation
(CAD). It is proposed that the effects of amide-to-ester bond substitution on fragmentation are mainly due to the differences
in product ion stability (ECD, CAD) as well as proton affinity (CAD). This proposal is substantiated by calculations using
density functional theory. The implications of these results in relation to the current understanding of the mechanisms of
electron capture dissociation and electron transfer dissociation are discussed. 相似文献
14.
Electron capture dissociation (ECD) offers many advantages over the more traditional fragmentation techniques for the analysis of peptides and proteins, although the question remains: How suitable is ECD for incorporation within proteomic strategies for the identification of proteins? Here, we compare LC-ECD-MS/MS and LC-CID-MS/MS as techniques for the identification of proteins. Experiments were performed on a hybrid linear ion trap-Fourier transform ion cyclotron resonance mass spectrometer. Replicate analyses of a six-protein (bovine serum albumin, apo-transferrin, lysozyme, cytochrome c, alcohol dehydrogenase, and β-galactosidase) tryptic digest were performed and the results analyzed on the basis of overall protein sequence coverage and sequence tag lengths within individual peptides. The results show that although protein coverage was lower for LC-ECD-MS/MS than for LC-CID-MS/MS, LC-ECD-MS/MS resulted in longer peptide sequence tags, providing greater confidence in protein assignment. 相似文献
15.
Zirah S Afonso C Linne U Knappe TA Marahiel MA Rebuffat S Tabet JC 《Journal of the American Society for Mass Spectrometry》2011,22(3):467-479
Lasso peptides constitute a class of bioactive peptides sharing a knotted structure where the C-terminal tail of the peptide is threaded through and trapped within an N-terminal macrolactam ring. The structural characterization of lasso structures and differentiation from their unthreaded
topoisomers is not trivial and generally requires the use of complementary biochemical and spectroscopic methods. Here we
investigated two antimicrobial peptides belonging to the class II lasso peptide family and their corresponding unthreaded
topoisomers: microcin J25 (MccJ25), which is known to yield two-peptide product ions specific of the lasso structure under
collision-induced dissociation (CID), and capistruin, for which CID does not permit to unambiguously assign the lasso structure.
The two pairs of topoisomers were analyzed by electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry
(ESI-FTICR MS) upon CID, infrared multiple photon dissociation (IRMPD), and electron capture dissociation (ECD). CID and ECD
spectra clearly permitted to differentiate MccJ25 from its non-lasso topoisomer MccJ25-Icm, while for capistruin, only ECD
was informative and showed different extent of hydrogen migration (formation of c•/z from c/z•) for the threaded and unthreaded topoisomers. The ECD spectra of the triply-charged MccJ25 and MccJ25-lcm showed a series
of radical b-type product ions ( b¢n · ) \left( {b{\prime}_n^{ \bullet }} \right) . We proposed that these ions are specific of cyclic-branched peptides and result from a dual c/z• and y/b dissociation, in
the ring and in the tail, respectively. This work shows the potentiality of ECD for structural characterization of peptide
topoisomers, as well as the effect of conformation on hydrogen migration subsequent to electron capture. 相似文献
16.
Deguchi K Ito H Baba T Hirabayashi A Nakagawa H Fumoto M Hinou H Nishimura S 《Rapid communications in mass spectrometry : RCM》2007,21(5):691-698
Structural analyses of various glycans attached to proteins and peptides are highly desirable for elucidating their biological roles. An approach based on mass spectrometry (MS) combining both collision-induced dissociation (CID) and electron-capture dissociation (ECD) in the positive- and negative-ion modes has been proposed as a simple and direct method of assigning an O-glycan without releasing it from the peptide and of determining the amino acid sequence of the peptide and glycosylation site. The instrument used is an electrospray ionization (ESI) linear ion trap (LIT) time-of-flight (TOF) mass spectrometer with tandem LITs for CID by He gas and ECD. The proposed approach was tested with two synthetic O-glycopeptides binding a sialyl Lewis x (sLe(x)) oligosaccharide and a 3'-sialyl N-acetyllactosamine (3'-SLN) on a serine (S) residue. In the negative-ion mode, the CID MS(2) spectra of O-glycopeptides showed a relatively abundant glycoside-bond cleavage between the core N-acetylglucosamine (GlcNAc) and serine (S) that yields deprotonated C(3)-type fragment ions of O-glycan and deprotonated Z(0)-type peptide ions. The structure of the sLe(x) (3'-SLN) oligosaccharide was simply assigned by comparing the CID MS(3) spectrum derived from the C(3)-type fragment ion with the CID MS(2) spectra of the sLe(x) and sLe(a) (3'- and 6'-SLN) standards (i.e., negative-ion MS(n) spectral matching). The amino acid sequence of the peptide including the glycosylation site was determined from the ECD MS(2) spectrum in the positive-ion mode. 相似文献
17.
Victor A. Mikhailov Helen J. Cooper 《Journal of the American Society for Mass Spectrometry》2009,20(5):763-771
Here, we show that to perform activated ion electron capture dissociation (AI-ECD) in a Fourier transform ion cyclotron resonance
(FT-ICR) mass spectrometer equipped with a CO2 laser, it is necessary to synchronize both infrared irradiation and electron capture dissociation with ion magnetron motion.
This requirement is essential for instruments in which the infrared laser is angled off-axis, such as the Thermo Finnigan
LTQ FT. Generally, the electron irradiation time required for proteins is much shorter (ms) than that required for peptides
(tens of ms), and the modulation of ECD, AI ECD, and infrared multiphoton dissociation (IRMPD) with ion magnetron motion is
more pronounced. We have optimized AI ECD for ubiquitin, cytochrome c, and myoglobin; however the results can be extended to other proteins. We demonstrate that pre-ECD and post-ECD activation
are physically different and display different kinetics. We also demonstrate how, by use of appropriate AI ECD time sequences
and normalization, the kinetics of protein gas-phase refolding can be deconvoluted from the diffusion of the ion cloud and
measured on the time scale longer than the period of ion magnetron motion. 相似文献
18.
Chamot-Rooke J van der Rest G Dalleu A Bay S Lemoine J 《Journal of the American Society for Mass Spectrometry》2007,18(8):1405-1413
Electron capture dissociation (ECD) has become an alternative method to collision-activated dissociation (CAD) to avoid gas-phase cleavage of post-translational modifications carried by side chains from the peptide backbone. Nonetheless, as illustrated herein by the study of O-glycosylated and O-phosphorylated peptides, the extent of ECD fragmentations may be insufficient to cover the entire peptide sequence and to localize accurately these modifications. The present work demonstrates that the derivatization of peptides at their N-terminus by a phosphonium group improves dramatically and systematically the sequence coverage deduced from the ECD spectrum for both O-glycosylated and O-phosphorylated peptides compared with their native counterparts. The exclusive presence of N-terminal fragments (c-type ions) in the ECD spectra of doubly charged molecular cations simplifies peptide sequence interpretation. Thus, the combination of ECD and fixed charge derivatization appears as an efficient analytical tool for the extensive sequencing of peptides bearing labile groups. 相似文献
19.
Information about protein conformation can be obtained with hydrogen/deuterium exchange (HDX) mass spectrometry. The isotopic solution-phase exchange of specific amide hydrogen atoms can be followed using low-vacuum nozzle-skimmer collision-induced dissociation (CID). In this study, the nozzle-skimmer technique was complemented by electron capture dissociation (ECD) Fourier transform ion cyclotron resonance mass spectrometry (FTICRMS). The solution-phase exchange at a specific residue is monitored by comparing isotopic distributions of two consecutive b- or c-type ions. While nozzle-skimmer fragmentation takes place in the low-vacuum region of the mass spectrometer, ECD occurs at ultra-high vacuum within the mass analyzer cell of the FTICR mass spectrometer. The dissociations take place at 10(-4) and 10(-9) mbar, respectively. Low-vacuum nozzle-skimmer fragmentation can result in intramolecular exchange between product ions and solvent molecules in the gas phase. Consequently, the solution-phase information about protein or peptide conformation is lost. It was not possible to monitor isotopic solution-phase exchange at the eighth residue in substance P, (Phe)8, with nozzle-skimmer CID. By using the in-cell ECD fragmentation method, the solution-phase exchange at the (Phe)8 residue was preserved during mass spectrometric analysis. This result shows the complementary aspects of applying fragmentation at low and at high vacuum, when studying isotopic exchange in solution at specific residues using FTICRMS. 相似文献
20.
Mitsuo Takayama Sadanori Sekiya Ryunosuke Iimuro Shinichi Iwamoto Koichi Tanaka 《Journal of the American Society for Mass Spectrometry》2014,25(1):120-131
Selective and nonselective cleavages in ion trap low-energy collision-induced dissociation (CID) experiments of the fragments generated from in-source decay (ISD) with matrix-assisted laser desorption/ionization mass spectrometry (MALDI MS) of intact proteins are described in both positive and negative ion modes. The MALDI-ISD spectra of the proteins demonstrate common, discontinuous, abundant c- and z′-ions originating from cleavage at the N–Cα bond of Xxx-Asp/Asn and Gly-Xxx residues in both positive- and negative-ion modes. The positive ion CID of the c- and z′-ions resulted in product ions originating from selective cleavage at Asp-Xxx, Glu-Xxx and Cys-Xxx residues. Nonselective cleavage product ions rationalized by the mechanism of a “mobile proton” are also observed in positive ion CID spectra. Negative ion CID of the ISD fragments results in complex product ions accompanied by the loss of neutrals from b-, c-, and y-ions. The most characteristic feature of negative ion CID is selective cleavage of the peptide bonds of acidic residues, Xxx-Asp/Glu/Cys. A definite influence of α-helix on the CID product ions was not obtained. However, the results from positive ion and negative ion CID of the MALDI-ISD fragments that may have long α-helical domains suggest that acidic residues in helix-free regions tend to degrade more than those in helical regions. Figure
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