Identification and characterization of the direct folding process of hen egg-white lysozyme
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00530a007
Reference25 articles.
1. Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
2. Role of proline isomerization in folding of ribonuclease A at low temperatures
3. Both the Fast and Slow Refolding Reactions of Ribonuclease A Yield Native Enzyme
4. The heat-unfolded state of ribonuclease A is an equilibrium mixture of fast and slow refolding species
5. A physical difference between the fast- and slow-refolding forms of nitrotyrosyl ribonuclease A: the pK values of the nitrotyrosyl groups
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1. The thermodynamics of protein folding: a critique of widely used quasi-thermodynamic interpretations and a restatement based on the Gibbs–Duhem relation and consistent with the Phase Rule;Physical Chemistry Chemical Physics;2010
2. A near-native state on the slow refolding pathway of hen lysozyme;Protein Science;2008-12-31
3. Characterization of the transition state of Lysozyme unfolding. I. Effect of protein-solvent interactions on the transition state;Biopolymers;2007-09-21
4. A stopped-flow fluorescence study of the native and modified lysozyme;Biologia;2007-06
5. Sequential vs. parallel protein-folding mechanisms: experimental tests for complex folding reactions;Biophysical Chemistry;2002-12
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