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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Hydrogen-Deuterium Exchange of Lipoxygenase Uncovers a Relationship between Distal, Solvent Exposed Protein Motions and the Thermal Activation Barrier for Catalytic Proton-Coupled Electron Tunneling.
Adam R. Offenbacher,Adam R. Offenbacher,Shenshen Hu,Shenshen Hu,Erin M. Poss,Cody A. Marcus Carr,Cody A. Marcus Carr,Alexander D. Scouras,Alexander D. Scouras,Daniil M. Prigozhin,Daniil M. Prigozhin,Anthony T. Iavarone,Anthony T. Iavarone,Ali Palla,Tom Alber,Tom Alber,James S. Fraser,Judith P. Klinman,Judith P. Klinman +18 more
TL;DR: The application of hydrogen–deuterium exchange coupled to mass spectrometry toward the spatial resolution of protein motions that can be related to an enzyme’s catalytic parameters is presented.
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Effects of domain dissection on the folding and stability of the 43 kDa protein PGK probed by NMR
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Structural determinants for the binding of anthrax lethal factor to oligomeric protective antigen.
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Dissection of Conformational Conversion Events during Prion Amyloid Fibril Formation Using Hydrogen Exchange and Mass Spectrometry
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TL;DR: A detailed quantitative analysis of the NOE intensities observed in aqueous HFIP revealed alternative conformations in the C-terminal portion of the common amylin helix, a region that is known to be involved in the biorecognition phenomena leading to amyloidogenesis.
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