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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Halophilic Protein Adaptation Results from Synergistic Residue-Ion Interactions in the Folded and Unfolded States
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Unfolding and aggregation of a glycosylated monoclonal antibody on a cation exchange column. Part II. Protein structure effects by hydrogen deuterium exchange mass spectrometry.
Jing Guo,Giorgio Carta +1 more
TL;DR: Hydrogen-deuterium exchange mass spectrometry (HX-MS) with proteolytic fragmentation is used to determine patterns of unfolding, as measured by increased solvent exposure, with peptide-level resolution for a glycosylated monoclonal antibody both when eluted from a tentacle-type cation exchange column and while bound to the resin.
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MHC class II complexes sample intermediate states along the peptide exchange pathway.
Marek Wieczorek,Jana Sticht,Sebastian Stolzenberg,Sebastian Günther,Sebastian Günther,Christoph Wehmeyer,Zeina El Habre,Miguel Álvaro-Benito,Frank Noé,Christian Freund +9 more
TL;DR: Combining NMR-detected H/D exchange with Markov modelling analysis of an aggregate of 275 microseconds molecular dynamics simulations, it is revealed that a stable pMHCII spontaneously samples intermediate conformations relevant for peptide exchange.
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Ensemble modulation as an origin of denaturant-independent hydrogen exchange in proteins
TL;DR: A general thermodynamic description of HX is used to find that the denaturant dependence seen in HX experiments under native conditions is not a de facto indication of the amount of surface area exposure required for exchange.
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Conformational stability of HPr: The histidine‐containing phosphocarrier protein from Bacillus subtilis
TL;DR: In the presence of moderate concentrations of urea, HPr exhibits cold denaturation, and thus a complete stability curve for HPr, including a measure of delta Cp, can be achieved using the method of Chen and Schellman.
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