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A new method for the accurate determination of the isotopic state of single amide hydrogens within peptides using Fourier transform ion cyclotron resonance mass spectrometry
Author(s) -
Buijs Jos,
Håkansson Kristina,
Hagman Charlotte,
Håkansson Per,
Oscarsson Sven
Publication year - 2000
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/1097-0231(20001015)14:19<1751::aid-rcm89>3.0.co;2-t
Subject(s) - chemistry , fourier transform ion cyclotron resonance , mass spectrometry , amide , deuterium , hydrogen–deuterium exchange , fragmentation (computing) , analytical chemistry (journal) , ion cyclotron resonance , isotopic labeling , hydrogen , ion , chromatography , atomic physics , organic chemistry , cyclotron , physics , computer science , operating system
A new method is presented to accurately determine the probability of having a deuterium or hydrogen atom on a specific amide position within a peptide after deuterium/hydrogen (D/H) exchange in solution. Amide hydrogen exchange has been proven to be a sensitive probe for studying protein structures and structural dynamics. At the same time, mass spectrometry in combination with physical fragmentation methods is commonly used to sequence proteins based on an amino acid residue specific mass analysis. In the present study it is demonstrated that the isotopic patterns of a series of peptide fragment ions obtained with capillary‐skimmer dissociation, as observed with a 9.4 T Fourier transform ion cyclotron resonance (FTICR) mass spectrometer, can be used to calculate the isotopic state of specific amide hydrogens. This calculation is based on the experimentally observed isotopic patterns of two consecutive fragments and on the isotopic binomial distributions of the atoms in the residue constituting the difference between these two consecutive fragments. The applicability of the method is demonstrated by following the sequence‐specific D/H exchange rate in solution of single amide hydrogens within some peptides. Copyright © 2000 John Wiley & Sons, Ltd.