Comparison between the unfolding rate and structural fluctuations in native lysozyme?effects of denaturants, ligand binding, and intrachain cross-linking on hydrogen exchange and unfolding kinetics-Reference-Cited by-同舟云学术

Comparison between the unfolding rate and structural fluctuations in native lysozyme?effects of denaturants, ligand binding, and intrachain cross-linking on hydrogen exchange and unfolding kinetics

Published:1986-10 Issue:10 Volume:25 Page:1981-1996
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Segawa Shin-Ichi,Kume Katsuya

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Reference19 articles.

1. Energetics of protein structure and folding

2. Characterization of the transition state of Lysozyme unfolding. I. Effect of protein-solvent interactions on the transition state

3. Characterization of the distribution of internal motions in the basic pancreatic trypsin inhibitor using a large number of internal NMR probes

4. Amide-proton exchange studies by two-dimensional correlated 1H NMR in two chemically modified analogs of the basic pancreatic trypsin inhibitor

5. Hydrogen exchange and structural dynamics of proteins and nucleic acids

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3. A two-dimensional NMR study of exchange behavior of amide hydrogens in a lysozyme derivative with an extra cross-link between Glu35 and Trp 108—quenching of cooperative fluctuations and effects on the protein stability;Biopolymers;1997-02

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