Electronic Resource
College Park, Md.
:
American Institute of Physics (AIP)
The Journal of Chemical Physics
104 (1996), S. 3395-3398
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1063/1.471044
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