pH-Induced folding/unfolding of staphylococcal nuclease: determination of kinetic parameters by the sequential-jump method
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00120a027
Reference29 articles.
1. Hydrogen-1 NMR evidence for three interconverting forms of staphylococcal nuclease: effects of mutations and solution conditions on their distribution
2. Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig .alpha.-lactalbumin
3. Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
4. Kinetic analysis of the acid and the alkaline unfolded states of staphylococcal nuclease
5. A kinetic study of the folding of nuclease B, a possible precursor of staphylococcal nuclease A
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1. Hydrophobic condensation and modular assembly model of protein folding;Biosystems;2008-07
2. Compact dimension of denatured states of staphylococcal nuclease;Proteins: Structure, Function, and Bioinformatics;2008-02-14
3. A molecular dynamics simulation of SNase and its hydration shell at high temperature and high pressure;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2006-03
4. Design and Synthesis of a Chemically Cleavable Fluorescent Nucleotide, 3‘-O-Allyl-dGTP-allyl-Bodipy-FL-510, as a Reversible Terminator for DNA Sequencing by Synthesis;Journal of the American Chemical Society;2006-02-03
5. Local stability identification and the role of key acidic amino acid residues in staphylococcal nuclease unfolding;FEBS Journal;2005-07-19
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