Toward an outline of the topography of a realistic protein-folding funnel.

José N. Onuchic(University of Illinois Urbana-Champaign), Peter G. Wolynes(University of Illinois Urbana-Champaign), Zaida Luthey‐Schulten(University of Illinois Urbana-Champaign), Nicholas D. Socci(University of Illinois Urbana-Champaign)
Proceedings of the National Academy of Sciences
April 11, 1995
Cited by 523Open Access

Abstract

Experimental information on the structure and dynamics of molten globules gives estimates for the energy landscape's characteristics for folding highly helical proteins, when supplemented by a theory of the helix-coil transition in collapsed heteropolymers. A law of corresponding states relating simulations on small lattice models to real proteins possessing many more degrees of freedom results. This correspondence reveals parallels between "minimalist" lattice results and recent experimental results for the degree of native character of the folding transition state and molten globule and also pinpoints the needs of further experiments.


Related Papers

No related papers found

Powered by citation graph analysis