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GroEL-mediated protein folding.
Protein Sci. 1997 Apr; 6(4):743-60.PS

Abstract

I. Architecture of GroEL and GroES and the reaction pathway A. Architecture of the chaperonins B. Reaction pathway of GroEL-GroES-mediated folding II. Polypeptide binding A. A parallel network of chaperones binding polypeptides in vivo B. Polypeptide binding in vitro 1. Role of hydrophobicity in recognition 2. Homologous proteins with differing recognition-differences in primary structure versus effects on folding pathway 3. Conformations recognized by GroEL a. Refolding studies b. Binding of metastable intermediates c. Conformations while stably bound at GroEL 4. Binding constants and rates of association 5. Conformational changes in the substrate protein associated with binding by GroEL a. Observations b. Kinetic versus thermodynamic action of GroEL in mediating unfolding c. Crossing the energy landscape in the presence of GroEL III. ATP binding and hydrolysis-driving the reaction cycle IV. GroEL-GroES-polypeptide ternary complexes-the folding-active cis complex A. Cis and trans ternary complexes B. Symmetric complexes C. The folding-active intermediate of a chaperonin reaction-cis ternary complex D. The role of the cis space in the folding reaction E. Folding governed by a "timer" mechanism F. Release of nonnative polypeptides during the GroEL-GroES reaction G. Release of both native and nonnative forms under physiologic conditions H. A role for ATP binding, as well as hydrolysis, in the folding cycle V. Concluding remarks.

Authors+Show Affiliations

Department of Genetics, Yale School of Medicine, New Haven, Connecticut 06510, USA.No affiliation info available

Pub Type(s)

Journal Article
Review

Language

eng

PubMed ID

9098884

Citation

Fenton, W A., and A L. Horwich. "GroEL-mediated Protein Folding." Protein Science : a Publication of the Protein Society, vol. 6, no. 4, 1997, pp. 743-60.
Fenton WA, Horwich AL. GroEL-mediated protein folding. Protein Sci. 1997;6(4):743-60.
Fenton, W. A., & Horwich, A. L. (1997). GroEL-mediated protein folding. Protein Science : a Publication of the Protein Society, 6(4), 743-60.
Fenton WA, Horwich AL. GroEL-mediated Protein Folding. Protein Sci. 1997;6(4):743-60. PubMed PMID: 9098884.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - GroEL-mediated protein folding. AU - Fenton,W A, AU - Horwich,A L, PY - 1997/4/1/pubmed PY - 1997/4/1/medline PY - 1997/4/1/entrez SP - 743 EP - 60 JF - Protein science : a publication of the Protein Society JO - Protein Sci VL - 6 IS - 4 N2 - I. Architecture of GroEL and GroES and the reaction pathway A. Architecture of the chaperonins B. Reaction pathway of GroEL-GroES-mediated folding II. Polypeptide binding A. A parallel network of chaperones binding polypeptides in vivo B. Polypeptide binding in vitro 1. Role of hydrophobicity in recognition 2. Homologous proteins with differing recognition-differences in primary structure versus effects on folding pathway 3. Conformations recognized by GroEL a. Refolding studies b. Binding of metastable intermediates c. Conformations while stably bound at GroEL 4. Binding constants and rates of association 5. Conformational changes in the substrate protein associated with binding by GroEL a. Observations b. Kinetic versus thermodynamic action of GroEL in mediating unfolding c. Crossing the energy landscape in the presence of GroEL III. ATP binding and hydrolysis-driving the reaction cycle IV. GroEL-GroES-polypeptide ternary complexes-the folding-active cis complex A. Cis and trans ternary complexes B. Symmetric complexes C. The folding-active intermediate of a chaperonin reaction-cis ternary complex D. The role of the cis space in the folding reaction E. Folding governed by a "timer" mechanism F. Release of nonnative polypeptides during the GroEL-GroES reaction G. Release of both native and nonnative forms under physiologic conditions H. A role for ATP binding, as well as hydrolysis, in the folding cycle V. Concluding remarks. SN - 0961-8368 UR - https://www.unboundmedicine.com/medline/citation/9098884/GroEL_mediated_protein_folding_ DB - PRIME DP - Unbound Medicine ER -