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Characterization of peptide folding nuclei by hydrogen/deuterium exchange‐mass spectrometry
Author(s) -
Li Xue,
Hood Robin J.,
Wedemeyer William J.,
Watson J. Throck
Publication year - 2005
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.051458905
Subject(s) - chemistry , mass spectrometry , hydrogen–deuterium exchange , protein secondary structure , tandem mass spectrometry , protein mass spectrometry , peptide , circular dichroism , deuterium , folding (dsp implementation) , protein folding , protein tertiary structure , crystallography , chromatography , biochemistry , physics , quantum mechanics , electrical engineering , engineering
Covalently linked pairs of well‐chosen peptides can be good model systems for protein folding studies because they can adopt stable secondary, side‐chain, and tertiary structure under certain conditions. We demonstrate a method for characterizing the structure in such peptide pairs by hydrogen/deuterium exchange of individual amide groups analyzed by collision‐induced dissociation tandem mass spectrometry, in concert with circular dichroism spectroscopy. We apply the method to two peptides (and their three possible pairs) from bovine pancreatic trypsin inhibitor to address specific hypotheses regarding the stabilization of local secondary structure by long‐range interactions.