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Ion‐molecule reactions as probes of gas‐phase structures of peptides and proteins
Author(s) -
Green M. Kirk,
Lebrilla Carlito B.
Publication year - 1997
Publication title -
mass spectrometry reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 126
eISSN - 1098-2787
pISSN - 0277-7037
DOI - 10.1002/(sici)1098-2787(1997)16:2<53::aid-mas1>3.0.co;2-8
Subject(s) - chemistry , protonation , affinities , proton affinity , molecule , hydrogen–deuterium exchange , deuterium , proton , ion , amino acid , ionic bonding , gas phase , intermolecular force , reagent , hydrogen bond , computational chemistry , hydrogen , stereochemistry , organic chemistry , biochemistry , physics , quantum mechanics
A review with over 100 references describes the recent applications of ion‐molecule reactions to the study of gas‐phase protonated peptides and proteins. The topic is focused specifically on the proton transfer and hydrogen‐deuterium exchange reactions of amino acids, peptides, and proteins. A brief background is given of the various methods used for assigning proton affinities and gas‐phase basicities. The methods used for measuring the kinetics of deuterium incorporation of charged ion in the presence of a background pressure of deuterating reagents are also described. Ion‐molecule reactions are used to determine, among other things, the gas‐phase basicities and proton affinities of amino acids, peptides, and proteins, the sites of protonation, intra‐ and intermolecular interactions, and conformational differences and changes in gas‐phase ionic species. Singly charged and multiply charged ions are both covered. © 1997 John Wiley & Sons, Inc., Mass Spectrom Rev 16(2), 53–71, 1997