Relationship between Kinetic and Equilibrium Folding Intermediates of Creatine Kinase
- 27 July 2001
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 285 (4) , 857-862
- https://doi.org/10.1006/bbrc.2001.5248
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- How do small single-domain proteins fold?Folding and Design, 1998
- Denaturation by guanidinium chloride of dimeric MM-creatine kinase and its proteinase K-nicked form: evidence for a multiple-step processBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1997
- Rapid formation of a molten globule intermediate in refolding of α-lactalbuminFolding and Design, 1996
- Compact Intermediates States in Protein FoldingPublished by Springer Nature ,1995
- Molten Globule and Protein FoldingPublished by Elsevier ,1995
- PATHWAYS OF PROTEIN FOLDINGAnnual Review of Biochemistry, 1993
- Protein folding: local structures, domains, subunits, and assembliesBiochemistry, 1991
- INTERMEDIATES IN THE FOLDING REACTIONS OF SMALL PROTEINSAnnual Review of Biochemistry, 1990
- The refolding of denatured rabbit muscle creatine kinase. Search for intermediates in the refolding process and effect of modification at the reactive thiol group on refoldingBiochemical Journal, 1982
- The refolding of denatured rabbit muscle creatine kinaseBiochimica et Biophysica Acta (BBA) - Protein Structure, 1980