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Extensive misfolding in the refolding reaction of alkaline ferrocytochrome C.
Biochemistry. 2006 Jul 11; 45(27):8393-401.B

Abstract

This work describes an extensively misfolded kinetic intermediate in the folding of horse ferrocytochrome c. Under absolute native conditions, the alkali-unfolded protein liganded with carbon-monoxide exhibits misfolding. The misfolded product, apparently an off-pathway intermediate, requires large-scale unfolding in order to have a chance to fold correctly to the native state. The rate of unfolding of the misfolded intermediate limits the overall rate of protein folding. The high level of observed misfolding possibly results from a failure of the polypeptide chain to achieve by stochastic search the transition state relevant for successful folding. Such misfolding may be analogous to the failure of a sizable set of proteins in the intracellular milieu to fold to the functionally active native state.

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

16819838

Citation

Rao, D Krishna, et al. "Extensive Misfolding in the Refolding Reaction of Alkaline Ferrocytochrome C." Biochemistry, vol. 45, no. 27, 2006, pp. 8393-401.
Rao DK, Prabhu NP, Bhuyan AK. Extensive misfolding in the refolding reaction of alkaline ferrocytochrome C. Biochemistry. 2006;45(27):8393-401.
Rao, D. K., Prabhu, N. P., & Bhuyan, A. K. (2006). Extensive misfolding in the refolding reaction of alkaline ferrocytochrome C. Biochemistry, 45(27), 8393-401.
Rao DK, Prabhu NP, Bhuyan AK. Extensive Misfolding in the Refolding Reaction of Alkaline Ferrocytochrome C. Biochemistry. 2006 Jul 11;45(27):8393-401. PubMed PMID: 16819838.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Extensive misfolding in the refolding reaction of alkaline ferrocytochrome C. AU - Rao,D Krishna, AU - Prabhu,N Prakash, AU - Bhuyan,Abani K, PY - 2006/7/6/pubmed PY - 2006/8/26/medline PY - 2006/7/6/entrez SP - 8393 EP - 401 JF - Biochemistry JO - Biochemistry VL - 45 IS - 27 N2 - This work describes an extensively misfolded kinetic intermediate in the folding of horse ferrocytochrome c. Under absolute native conditions, the alkali-unfolded protein liganded with carbon-monoxide exhibits misfolding. The misfolded product, apparently an off-pathway intermediate, requires large-scale unfolding in order to have a chance to fold correctly to the native state. The rate of unfolding of the misfolded intermediate limits the overall rate of protein folding. The high level of observed misfolding possibly results from a failure of the polypeptide chain to achieve by stochastic search the transition state relevant for successful folding. Such misfolding may be analogous to the failure of a sizable set of proteins in the intracellular milieu to fold to the functionally active native state. SN - 0006-2960 UR - https://www.unboundmedicine.com/medline/citation/16819838/Extensive_misfolding_in_the_refolding_reaction_of_alkaline_ferrocytochrome_C_ L2 - https://doi.org/10.1021/bi060141z DB - PRIME DP - Unbound Medicine ER -