Fast-folding experiments and the topography of protein folding energy landscapes

P. G. Wolynes; Z. Luthey-Schulten; J. N. Onuchic

doi:10.1016/S1074-5521(96)90090-3

Fast-folding experiments and the topography of protein folding energy landscapes

P. G. Wolynes, Z. Luthey-Schulten, J. N. Onuchic

Research output: Contribution to journal › Review article › peer-review

Abstract

The rapid folding of certain proteins can be described theoretically using an energy landscape in the shape of a folding funnel. New techniques have allowed the examination of fast-folding events that occur in microseconds or less, and have tested the predictions of the theoretical models.

Original language	English (US)
Pages (from-to)	425-432
Number of pages	8
Journal	Chemistry and Biology
Volume	3
Issue number	6
DOIs	https://doi.org/10.1016/S1074-5521(96)90090-3
State	Published - 1996

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Pharmacology
Drug Discovery
Clinical Biochemistry

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10.1016/S1074-5521(96)90090-3

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title = "Fast-folding experiments and the topography of protein folding energy landscapes",

abstract = "The rapid folding of certain proteins can be described theoretically using an energy landscape in the shape of a folding funnel. New techniques have allowed the examination of fast-folding events that occur in microseconds or less, and have tested the predictions of the theoretical models.",

author = "Wolynes, {P. G.} and Z. Luthey-Schulten and Onuchic, {J. N.}",

note = "The work at the University of California at San Diego was supported by the NSF (Grant No. MCB-93-16186) and at Illinois by the NIH (Grant No. 2 ROI GM44557).",

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AU - Wolynes, P. G.

AU - Luthey-Schulten, Z.

AU - Onuchic, J. N.

N1 - The work at the University of California at San Diego was supported by the NSF (Grant No. MCB-93-16186) and at Illinois by the NIH (Grant No. 2 ROI GM44557).

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Y1 - 1996

N2 - The rapid folding of certain proteins can be described theoretically using an energy landscape in the shape of a folding funnel. New techniques have allowed the examination of fast-folding events that occur in microseconds or less, and have tested the predictions of the theoretical models.

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Fast-folding experiments and the topography of protein folding energy landscapes

Abstract

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