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A thermodynamic coupling mechanism can explain the GroEL-mediated acceleration of the folding of barstar.
J Mol Biol. 2000 Apr 14; 297(5):1037-44.JM

Abstract

Despite extensive structural and kinetic studies, the mechanism by which the Escherichia coli chaperonin GroEL assists protein folding has remained somewhat elusive. It appears that GroEL might play an active role in facilitating folding, in addition to its role in restricting protein aggregation by secluding folding intermediates. We have investigated the kinetic mechanism of GroEL-mediated refolding of the small protein barstar. GroEL accelerates the observed fast (millisecond) refolding rate, but it does not affect the slow refolding kinetics. A thermodynamic coupling mechanism, in which the concentration of exchange-competent states is increased by the law of mass action, can explain the enhancement of the fast refolding rates. It is not necessary to invoke a catalytic role for GroEL, whereby either the intrinsic refolding rate of a productive folding transition or the unfolding rate of a kinetically trapped off-pathway intermediate is increased by the chaperonin.

Authors+Show Affiliations

National Centre for Biological Sciences, Tata Institute of Fundamental Research, UAS-GKVK Campus, Bangalore, 5600065, India.No affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

10764571

Citation

Bhutani, N, and J B. Udgaonkar. "A Thermodynamic Coupling Mechanism Can Explain the GroEL-mediated Acceleration of the Folding of Barstar." Journal of Molecular Biology, vol. 297, no. 5, 2000, pp. 1037-44.
Bhutani N, Udgaonkar JB. A thermodynamic coupling mechanism can explain the GroEL-mediated acceleration of the folding of barstar. J Mol Biol. 2000;297(5):1037-44.
Bhutani, N., & Udgaonkar, J. B. (2000). A thermodynamic coupling mechanism can explain the GroEL-mediated acceleration of the folding of barstar. Journal of Molecular Biology, 297(5), 1037-44.
Bhutani N, Udgaonkar JB. A Thermodynamic Coupling Mechanism Can Explain the GroEL-mediated Acceleration of the Folding of Barstar. J Mol Biol. 2000 Apr 14;297(5):1037-44. PubMed PMID: 10764571.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A thermodynamic coupling mechanism can explain the GroEL-mediated acceleration of the folding of barstar. AU - Bhutani,N, AU - Udgaonkar,J B, PY - 2000/4/15/pubmed PY - 2000/4/15/medline PY - 2000/4/15/entrez SP - 1037 EP - 44 JF - Journal of molecular biology JO - J Mol Biol VL - 297 IS - 5 N2 - Despite extensive structural and kinetic studies, the mechanism by which the Escherichia coli chaperonin GroEL assists protein folding has remained somewhat elusive. It appears that GroEL might play an active role in facilitating folding, in addition to its role in restricting protein aggregation by secluding folding intermediates. We have investigated the kinetic mechanism of GroEL-mediated refolding of the small protein barstar. GroEL accelerates the observed fast (millisecond) refolding rate, but it does not affect the slow refolding kinetics. A thermodynamic coupling mechanism, in which the concentration of exchange-competent states is increased by the law of mass action, can explain the enhancement of the fast refolding rates. It is not necessary to invoke a catalytic role for GroEL, whereby either the intrinsic refolding rate of a productive folding transition or the unfolding rate of a kinetically trapped off-pathway intermediate is increased by the chaperonin. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/10764571/A_thermodynamic_coupling_mechanism_can_explain_the_GroEL_mediated_acceleration_of_the_folding_of_barstar_ DB - PRIME DP - Unbound Medicine ER -