Folding intermediates of wild-type and mutants of barnase. I. use of φ-value analysis and m-values to probe the cooperative nature of the folding pre-equilibrium-Reference-Cited by-同舟云学术

Folding intermediates of wild-type and mutants of barnase. I. use of φ-value analysis and m-values to probe the cooperative nature of the folding pre-equilibrium

Published:1998-02 Issue:3 Volume:276 Page:625-646
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Dalby Paul A.,Oliveberg Mikael,Fersht Alan R.

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference27 articles.

1. A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR;Arcus;J. Mol. Biol.,1995

2. Denatured states of proteins;Dill;Annu. Rev. Biochem.,1991

3. Kinetic consequences of the removal of a disulfide bridge on the folding of hen lysozyme;Eyles;Biochemistry,1994

4. The sixth Datta lecture. Protein folding and stability;Fersht;FEBS Letters,1993

5. Nucleation mechanisms in protein folding;Fersht;Curr. Opin. Struct. Biol.,1997

Cited by 57 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. From covalent transition states in chemistry to noncovalent in biology: from β- to Φ-value analysis of protein folding;Quarterly Reviews of Biophysics;2024

2. Substitutions of Amino Acids with Large Number of Contacts in the Native State Have no Effect on the Rates of Protein Folding;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2016-12

3. Thermodynamics of protein destabilization in live cells;Proceedings of the National Academy of Sciences;2015-09-21

4. Recognition of protein folding kinetics pathways based on amino acid properties information derived from primary sequence;Chemometrics and Intelligent Laboratory Systems;2013-07

5. Three-state thermal unfolding of onconase;Biophysical Chemistry;2011-12