Transition State Characterization of the Low- to Physiological-Temperature Nondenaturational Conformational Change in Bovine Adenosine Deaminase by Slow Scan Rate Differential Scanning Calorimetry-Reference-Cited by-同舟云学术

Transition State Characterization of the Low- to Physiological-Temperature Nondenaturational Conformational Change in Bovine Adenosine Deaminase by Slow Scan Rate Differential Scanning Calorimetry

Published:2006-03-31 Issue:2 Volume:39 Page:167-170
ISSN:1976-6696
Container-title:BMB Reports
language:en
Short-container-title:BMB Reports

Author:

Bodnar Melissa A.,Britt B. Mark

Publisher

Korean Society for Biochemistry and Molecular Biology - BMB Reports

Subject

Molecular Biology,Biochemistry,General Medicine

Link

http://ocean.kisti.re.kr/downfile/crosscheck/ksbmb/JAKO200609137569479.pdf

Reference9 articles.

1. Low-temperature unfolding of a mutant of phage T4 lysozyme. 1. Equilibrium studies

2. Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations

3. Scan-rate dependence in protein calorimetry: The reversible transitions ofBacillus circulansxylanase and a disulfide-bridge mutant

4. Calculation of protein extinction coefficients from amino acid sequence data

5. Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation

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1. Thermodynamic analysis of the nondenaturational conformational change of baker’s yeast phosphoglycerate kinase at 24°C;Archives of Biochemistry and Biophysics;2008-10

2. Partial Phase Diagram of Aqueous Bovine Carbonic Anhydrase: Analyses of the Pressure-Dependent Temperatures of the Low- to Physiological-Temperature Nondenaturational Conformational Change and of Unfolding to the Molten Globule State;Journal of Biomolecular Structure and Dynamics;2008-10