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Internal friction controls the speed of protein folding from a compact configuration.
Biochemistry. 2004 Oct 05; 43(39):12532-8.B

Abstract

Several studies have found millisecond protein folding reactions to be controlled by the viscosity of the solvent: Reducing the viscosity allows folding to accelerate. In the limit of very low solvent viscosity, however, one expects a different behavior. Internal interactions, occurring within the solvent-excluded interior of a compact molecule, should impose a solvent-independent upper limit to folding speed once the bulk diffusional motions become sufficiently rapid. Why has this not been observed? We have studied the effect of solvent viscosity on the folding of cytochrome c from a highly compact, late-stage intermediate configuration. Although the folding rate accelerates as the viscosity declines, it tends toward a finite limiting value approximately 10(5) s(-1) as the viscosity tends toward zero. This limiting rate is independent of the cosolutes used to adjust solvent friction. Therefore, interactions within the interior of a compact denatured polypeptide can limit the folding rate, but the limiting time scale is very fast. It is only observable when the solvent-controlled stages of folding are exceedingly rapid or else absent. Interestingly, we find a very strong temperature dependence in these "internal friction"-controlled dynamics, indicating a large energy scale for the interactions that govern reconfiguration within compact, near-native states of a protein.

Authors+Show Affiliations

Department of Physics, University of Florida, P.O. Box 118440, Gainesville, Florida 32611-8440, USA.No affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

15449942

Citation

Pabit, Suzette A., et al. "Internal Friction Controls the Speed of Protein Folding From a Compact Configuration." Biochemistry, vol. 43, no. 39, 2004, pp. 12532-8.
Pabit SA, Roder H, Hagen SJ. Internal friction controls the speed of protein folding from a compact configuration. Biochemistry. 2004;43(39):12532-8.
Pabit, S. A., Roder, H., & Hagen, S. J. (2004). Internal friction controls the speed of protein folding from a compact configuration. Biochemistry, 43(39), 12532-8.
Pabit SA, Roder H, Hagen SJ. Internal Friction Controls the Speed of Protein Folding From a Compact Configuration. Biochemistry. 2004 Oct 5;43(39):12532-8. PubMed PMID: 15449942.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Internal friction controls the speed of protein folding from a compact configuration. AU - Pabit,Suzette A, AU - Roder,Heinrich, AU - Hagen,Stephen J, PY - 2004/9/29/pubmed PY - 2004/11/16/medline PY - 2004/9/29/entrez SP - 12532 EP - 8 JF - Biochemistry JO - Biochemistry VL - 43 IS - 39 N2 - Several studies have found millisecond protein folding reactions to be controlled by the viscosity of the solvent: Reducing the viscosity allows folding to accelerate. In the limit of very low solvent viscosity, however, one expects a different behavior. Internal interactions, occurring within the solvent-excluded interior of a compact molecule, should impose a solvent-independent upper limit to folding speed once the bulk diffusional motions become sufficiently rapid. Why has this not been observed? We have studied the effect of solvent viscosity on the folding of cytochrome c from a highly compact, late-stage intermediate configuration. Although the folding rate accelerates as the viscosity declines, it tends toward a finite limiting value approximately 10(5) s(-1) as the viscosity tends toward zero. This limiting rate is independent of the cosolutes used to adjust solvent friction. Therefore, interactions within the interior of a compact denatured polypeptide can limit the folding rate, but the limiting time scale is very fast. It is only observable when the solvent-controlled stages of folding are exceedingly rapid or else absent. Interestingly, we find a very strong temperature dependence in these "internal friction"-controlled dynamics, indicating a large energy scale for the interactions that govern reconfiguration within compact, near-native states of a protein. SN - 0006-2960 UR - https://www.unboundmedicine.com/medline/citation/15449942/Internal_friction_controls_the_speed_of_protein_folding_from_a_compact_configuration_ DB - PRIME DP - Unbound Medicine ER -