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Folding barrier in horse cytochrome c: support for a classical folding pathway.
J Mol Biol. 2004 Mar 12; 337(1):195-208.JM

Abstract

Native-state structures and conformations of ferrocytochrome c, nitrosylcytochrome c, and carbonmonoxycytochrome c are very similar. They are, however, immensely different from each other in terms of thermodynamic stability. The dramatic destabilization of ferrocytochrome c to the extent of 12 kcal mol(-1) produces no effect on the folding rate, and this is so in spite of the fact that all three test-tube variants fold in an apparent two-state manner. For all three proteins the folding barrier is early in time, sizable in energy, and is of the same magnitude (approximately 6.5 kcal mol(-1)). These results raise some challenges to the "new view" of protein folding. An early transition state, the search for which consumes most of the observed folding time, is suggested.

Authors+Show Affiliations

School of Chemistry, University of Hyderabad, Hyderabad 500046, India.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15001362

Citation

Prabhu, N Prakash, et al. "Folding Barrier in Horse Cytochrome C: Support for a Classical Folding Pathway." Journal of Molecular Biology, vol. 337, no. 1, 2004, pp. 195-208.
Prabhu NP, Kumar R, Bhuyan AK. Folding barrier in horse cytochrome c: support for a classical folding pathway. J Mol Biol. 2004;337(1):195-208.
Prabhu, N. P., Kumar, R., & Bhuyan, A. K. (2004). Folding barrier in horse cytochrome c: support for a classical folding pathway. Journal of Molecular Biology, 337(1), 195-208.
Prabhu NP, Kumar R, Bhuyan AK. Folding Barrier in Horse Cytochrome C: Support for a Classical Folding Pathway. J Mol Biol. 2004 Mar 12;337(1):195-208. PubMed PMID: 15001362.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Folding barrier in horse cytochrome c: support for a classical folding pathway. AU - Prabhu,N Prakash, AU - Kumar,Rajesh, AU - Bhuyan,Abani K, PY - 2003/08/12/received PY - 2004/01/07/revised PY - 2004/01/07/accepted PY - 2004/3/6/pubmed PY - 2004/4/9/medline PY - 2004/3/6/entrez SP - 195 EP - 208 JF - Journal of molecular biology JO - J Mol Biol VL - 337 IS - 1 N2 - Native-state structures and conformations of ferrocytochrome c, nitrosylcytochrome c, and carbonmonoxycytochrome c are very similar. They are, however, immensely different from each other in terms of thermodynamic stability. The dramatic destabilization of ferrocytochrome c to the extent of 12 kcal mol(-1) produces no effect on the folding rate, and this is so in spite of the fact that all three test-tube variants fold in an apparent two-state manner. For all three proteins the folding barrier is early in time, sizable in energy, and is of the same magnitude (approximately 6.5 kcal mol(-1)). These results raise some challenges to the "new view" of protein folding. An early transition state, the search for which consumes most of the observed folding time, is suggested. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/15001362/Folding_barrier_in_horse_cytochrome_c:_support_for_a_classical_folding_pathway_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022283604000622 DB - PRIME DP - Unbound Medicine ER -