Kinetics and Mechanism for the Formation of b- and y-type Ions from Singly Protonated Peptides on a Microsecond Time Scale: The Arginine Mystery

Product ion yields in postsource decay and time-resolved photodissociation at 193 and 266 nm were measured for some peptide ions with lysine ([KF6 + H]+, [F6K + H]+, and [F3KF3 + H]+) formed by matrix-assisted laser desorption ionization. The critical energy (E0) and entropy (DeltaS(double dagger)) were determined by RRKM fitting of the data. The results were similar to those found previously for peptide ions with histidine. To summarize, the presence of a basic residue, histidine or lysine, inside a peptide ion retarded its dissociation by lowering DeltaS(double dagger). On the basis of highly negative DeltaS(double dagger), presence of intramolecular interaction involving a basic group in the transition structure was proposed.

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Influence of basic residues on dissociation kinetics and dynamics of singly protonated peptides: time‐resolved photodissociation study

Yoon

Moon

Chung

et al. 2009

J. Mass Spectrom.

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Influence of charge distribution on the discrepant MS/MS fragmentation of the native and oxidized FMRF: evidence for the mobile proton model

Zong¹,

Liu²,

Sun³

et al. 2010

Journal of Peptide Science

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Using the mobile proton model as a framework, the influence of charge distribution on the discrepant fragmentation of peptides FMRF, FM(O)RF and FM(O(2))RF (with united peptide sequence) was explored by mass spectrometry experiments and quantum chemical calculations. With the added O atoms, more negative charges were prompted to deposit in the main protonation sites of the oxidation products. Consequently, the solvated proton to the oxidized peptides could flow to the amide bonds in an easier manner and made these bonds fragment easily. Oxidation also induced the discrepant fragmentation of these bonds in a predictable manner: the more negative charges deposited in an amide bond, the more daughter ions (a(n), b(n), y(n) ions and their derivatives) were produced. The combined methods proposed here refined the mobile proton model for peptide fragmentation and opened the way to probe the discrepant fragmentation of peptides in peptide/protein identification.

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Kinetics and Mechanism for the Formation of b- and y-type Ions from Singly Protonated Peptides on a Microsecond Time Scale: The Arginine Mystery

Cited by 2 publications

References 29 publications

Influence of basic residues on dissociation kinetics and dynamics of singly protonated peptides: time‐resolved photodissociation study

Influence of basic residues on dissociation kinetics and dynamics of singly protonated peptides: time‐resolved photodissociation study

Influence of charge distribution on the discrepant MS/MS fragmentation of the native and oxidized FMRF: evidence for the mobile proton model

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