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FAST KINETICS AND MECHANISMS IN PROTEIN FOLDING1 (2000)

Eaton, William A. ; Munoz, Victor ; Hagen, Stephen J. ; [et al.]

Palo Alto, Calif. : Annual Reviews

Annual Review of Biophysics and Biomolecular Structure 29 (2000), S. 327-359

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ISSN: 1056-8700

Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff

Topics: Biology , Physics

Notes: Abstract This review describes how kinetic experiments using techniques with dramatically improved time resolution have contributed to understanding mechanisms in protein folding. Optical triggering with nanosecond laser pulses has made it possible to study the fastest-folding proteins as well as fundamental processes in folding for the first time. These include formation of alpha-helices, beta-sheets, and contacts between residues distant in sequence, as well as overall collapse of the polypeptide chain. Improvements in the time resolution of mixing experiments and the use of dynamic nuclear magnetic resonance methods have also allowed kinetic studies of proteins that fold too fast (〉 103 s-1) to be observed by conventional methods. Simple statistical mechanical models have been extremely useful in interpreting the experimental results. One of the surprises is that models originally developed for explaining the fast kinetics of secondary structure formation in isolated peptides are also successful in calculating folding rates of single domain proteins from their native three-dimensional structure.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1146/annurev.biophys.29.1.327

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Nonexponential structural relaxations in proteins (1996)

Hagen, Stephen J. ; Eaton, William A.

College Park, Md. : American Institute of Physics (AIP)

The Journal of Chemical Physics 104 (1996), S. 3395-3398

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ISSN: 1089-7690

Source: AIP Digital Archive

Topics: Physics , Chemistry and Pharmacology

Notes: Conformational changes in proteins have been observed to exhibit a nonexponential time course. In myoglobin the conformational relaxation that follows photodissociation of the heme ligand is a very extended process that stretches from less than 1 picosecond to nearly 1 microsecond. We explain these kinetics with a model in which the initial protein conformational substates are connected to the final substates and to each other via transition states of a single energy. © 1996 American Institute of Physics.