ISSN:
0887-3585
Schlagwort(e):
protein structure
;
prediction
;
self-organization
;
stability
;
melting temperature
;
Chemistry
;
Biochemistry and Biotechnology
Quelle:
Wiley InterScience Backfile Collection 1832-2000
Thema:
Medizin
Notizen:
We have investigated the influence of the “noise” of inevitable errors in energetic parameters on-protein structure prediction. Because of this noise, only a part of all the interactions operating in a protein chain can be taken into account, and therefore a search for the energy minimum becomes inadequate for protein structure prediction. One can rather rely on statistical mechanics: a calculation carried out at a temperature T* somewhat below that of protein melting gives the best possible, though always approximate prediction. The early stages of protein folding also “take into account” only a part of all the interactions; consequently, the same temperature T* is favorable for the self-organization of native-like intermediates in protein folding. © 1995 Wiley-Liss, Inc.
Zusätzliches Material:
6 Ill.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1002/prot.340230205
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