Unfolding of chondroitinase ABC Ι is dependent on thermodynamic driving force by kinetically rate constant-amplitude compensation: A stopped-flow fluorescence study-Reference-Cited by-同舟云学术

Unfolding of chondroitinase ABC Ι is dependent on thermodynamic driving force by kinetically rate constant-amplitude compensation: A stopped-flow fluorescence study

Published:2016-11 Issue: Volume:93-94 Page:200-206
ISSN:0141-0229
Container-title:Enzyme and Microbial Technology
language:en
Short-container-title:Enzyme and Microbial Technology

Author:

Shirdel S. Akram,Khalifeh Khosrow^ORCID,Ranjbar Bijan,Golestani Abolfazl,Khajeh Khosro

Funder

Tarbiat Modares University

Publisher

Elsevier BV

Subject

Applied Microbiology and Biotechnology,Biochemistry,Biotechnology,Bioengineering

Reference29 articles.

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4. The folding of an enzyme: I. Theory of protein engineering analysis of stability and pathway of protein folding;Fersht;J. Mol. Riol.,1992

5. Non-prolyl cis-trans peptide bond isomerization as a rate-determining step in protein unfolding and refolding;Odefey;J. Mol. Biol.,1995

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