An equilibrium study of the dependence of secondary and tertiary structure of creatine kinase on subunit association
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference16 articles.
1. INTERMEDIATES IN THE FOLDING REACTIONS OF SMALL PROTEINS
2. [14]Determination and analysis of urea and guanidine hydrochloride denaturation curves
3. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
4. Kinetic evidence for active monomers during the reassembly of denatured creatine kinase
5. A comparison of native and covalently crosslinked creatine kinases: Denaturation and reassembly
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1. Conformational Change in the C-Terminal Domain Is Responsible for the Initiation of Creatine Kinase Thermal Aggregation;Biophysical Journal;2005-10
2. Effects of arginine on rabbit muscle creatine kinase and salt-induced molten globule-like state;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2003-11
3. Consequences of a six residual deletion from the N-terminal of rabbit muscle creatine kinase;Biochimie;2003-10
4. Studies on the stability of creatine kinase isozymes;Biochemistry and Cell Biology;2003-01-01
5. Stabilization of Creatine Kinase Encapsulated in Silicate Sol−Gel Materials and Unusual Temperature Effects on Its Activity;Chemistry of Materials;2002-09-24
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