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. 1995 Apr 11;92(8):3626–3630. doi: 10.1073/pnas.92.8.3626

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

J N Onuchic 1, P G Wolynes 1, Z Luthey-Schulten 1, N D Socci 1
PMCID: PMC42220  PMID: 7724609

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.

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Selected References

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