ISSN:
0887-3585
Keywords:
conformational changes
;
compact and flat native structures
;
metastable states
;
lattice model
;
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Medicine
Notes:
We present the results of lattice Monte Carlo simulations of protein folding in the framework of a model taking into account (i) the dependence of the energy of interaction of amino-acid residues on their orientation and (ii) the rigidity of the polypeptide chain with respect to the formation of kinks. If the chain is flexible, the final protein structures are predicted to be compact. Increasing the energy cost of creation of kinks is found to favor the formation of flat structures mimicking an ideal antiparallel β sheet. For compact structures, the kinetics of folding exhibit the standard two-phase regime (a rapid collapse to one of the metastable state, followed by slow reconfiguration of the chain to the native structure). For flat structures, the transition to the native state is often gradual. Proteins 29:508-516, 1997. © 1997 Wiley-Liss, Inc.
Additional Material:
11 Ill.
Type of Medium:
Electronic Resource
