Primary Structure Effects on Peptide Group Hydrogen Exchange
TLDR
The results provide the information necessary to evaluate measured protein NH to ND exchange rates by comparing them with rates to be expected for the same amino acid sequence is unstructured aligo‐ and polypeptides.Abstract:
The rate of exchange of peptide group NH hydrogens with the hydrogens of aqueous solvent is sensitive to neighboring side chains. To evaluate the effects of protein side chains, all 20 naturally occurring amino acids were studied using dipeptide models. Both inductive and steric blocking effects are apparent. The additivity of nearest-neighbor blocking and inductive effects was tested in oligo- and polypeptides and, surprisingly, confirmed. Reference rates for alanine-containing peptides were determined and effects of temperature considered. These results provide the information necessary to evaluate measured protein NH to ND exchange rates by comparing them with rates to be expected for the same amino acid sequence is unstructured oligo- and polypeptides. The application of this approach to protein studies is discussed.read more
Citations
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Journal ArticleDOI
Analytical Aspects of Hydrogen Exchange Mass Spectrometry
John R. Engen,Thomas E. Wales +1 more
TL;DR: The nature of analytical selectivity in hydrogen exchange is described, then the analytical tools required to accomplish fragmentation, separation, and the mass spectrometry measurements under restrictive exchange quench conditions are reviewed.
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The refolding of human lysozyme: a comparison with the structurally homologous hen lysozyme.
TL;DR: Results suggest that although the fundamental folding process is similar in the two proteins, human lysozyme differs in that it forms a stable subdomain involving the two N-terminal alpha-helices and the C-Terminal 3(10) helix in the first few milliseconds of folding, and that at least some tryptophan residues are ordered before the formation of the native state.
Journal ArticleDOI
Improved Protein Hydrogen/Deuterium Exchange Mass Spectrometry Platform with Fully Automated Data Processing
TL;DR: The improved HDX MS platform with fully automated data processing is described, which significantly reduces systematic and random errors in the measurement by introducing two types of corrections in HDX data analysis.
Journal ArticleDOI
Epitope mapping by amide hydrogen/deuterium exchange coupled with immobilization of antibody, on-line proteolysis, liquid chromatography and mass spectrometry.
TL;DR: The epitope of horse cytochrome c against monoclonal antibody E8 was determined using amide hydrogen/deuterium (H/D) exchange combined with immobilized antibody, on-line pepsin proteolysis, liquid chromatography (LC), and mass spectrometry (MS).
Journal ArticleDOI
Energetics of the interaction between water and the helical peptide group and its role in determining helix propensities
TL;DR: This work calculates the electrostatic solvation free energy (ESF) of the peptide groups in the helical and beta-strand conformations, by using the delphi program and parse parameter set, and shows that the ESF values of amides are almost entirely enthalpic.
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