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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Book ChapterDOI
Molten globule and protein folding.
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NMR Solution Structure of the Human Prion Protein
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References
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Journal ArticleDOI
Hydrogen-Tritium Exchange of the Random Chain Polypeptide
S.W. Englander,A. Poulsen +1 more
TL;DR: The hydrogen-tritium exchange character of poly-D,L-alanine was studied in detail as a model for the hydrogen exchange behavior of the polymeric peptide group as discussed by the authors.
Journal ArticleDOI
The Ionization Constant of Deuterium Oxide from 5 to 50
Journal ArticleDOI
Hydrogen exchange in native and denatured states of hen egg-white lysozyme.
Sheena E. Radford,Matthias Buck,Karen D. Topping,Christopher M. Dobson,Christopher M. Dobson,Philip A. Evans +5 more
TL;DR: The pattern of exchange rates from the native protein at high temperature, pH 3.8 69°C, resembles that of the acid‐denatured state, suggesting that under these conditions the exchange kinetics are dominated by transient global unfolding.
Journal ArticleDOI
Hydrogen exchange in thermally denatured ribonuclease A.
TL;DR: Hydrogen exchange has been used to test for the presence of nonrandom structure in thermally denatured ribonuclease A (RNase A) and the results show that exchange is approximately that predicted for a disordered polypeptide, but the predicted rates should be viewed with some caution.
Journal ArticleDOI
Detection and characterization of an early folding intermediate of T4 lysozyme using pulsed hydrogen exchange and two-dimensional NMR
Jirong Lu,Frederick W. Dahlquist +1 more
TL;DR: Two-dimensional 1H-15N NMR techniques combined with pulsed hydrogen-deuterium exchange have been used to characterize the folding pathway of T4 lysozyme and show that at least one intermediate is formed early during refolding at low denaturant concentrations.
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