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
Monitoring Hydrogen Exchange During Protein Folding by Fast Pressure Jump NMR Spectroscopy
TL;DR: A method is introduced that permits direct observation of the rates at which backbone amide hydrogens become protected from solvent exchange after rapidly dropping the hydrostatic pressure inside the NMR sample cell from denaturing to native conditions, indicating that the almost fully folded protein retains molten globule characteristics with severe NMR line broadening until the final hydrogen bonds are formed.
Journal ArticleDOI
Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR.
TL;DR: GroE, the chaperonin system of Escherichia coli, prevents the aggregation of partially folded or misfolded proteins by complexing them in a form competent for subsequent folding to the native state, and protection factors were found to be quite uniform along the sequence suggesting that CypA with native-like structure undergoes multiple cycles of unfolding while bound to GroEL, which are faster than unfolding in free solution.
Journal ArticleDOI
Impact of oxidation on protein therapeutics: Conformational dynamics of intact and oxidized acid-β-glucocerebrosidase at near-physiological pH
TL;DR: It appears that oxidation exerts its negative impact on the biological activity of GCase indirectly, primarily through accelerated aggregation and impaired trafficking.
Journal ArticleDOI
Solvent Exposed Non-contacting Amino Acids Play a Critical Role in NF-κB/IκBα Complex Formation
Tom Huxford,Dennis Mishler,Christopher B. Phelps,De-Bin Huang,Lei Lei Sengchanthalangsy,Ryan Reeves,Carrie A. Hughes,Elizabeth A. Komives,Gourisankar Ghosh +8 more
TL;DR: X-ray crystallographic and solvent accessibility experiments suggest that these solvent-exposed amino acid residues contribute to NF-κB/IκBα complex formation by modulating the NF-σκB p65 subunit NLS polypeptide.
Book ChapterDOI
Measurement of Solvent Accessibility at Protein-Protein Interfaces
TL;DR: It is shown that when the receptor is essentially 100% bound it is possible to distinguish amide exchange as a result of solvent accessibility at the interface from amid exchange caused by complex dissociation.
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