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Review
. 1999 Oct 12;96(21):11698-700.
doi: 10.1073/pnas.96.21.11698.

Go-ing for the prediction of protein folding mechanisms

S Takada  1
Affiliations
Review

Go-ing for the prediction of protein folding mechanisms

S Takada. Proc Natl Acad Sci U S A. .
No abstract available

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Figures

Figure 1
Figure 1
Schematic pictures of a statistical ensemble of proteins embedded in a folding funnel for a monomeric λ-repressor domain. At the top, the protein is in its denatured state and thus fluctuating wildly, where both energy and entropy are the largest. In the middle, the transition state forms a minicore made of helices 4 and 5 and a central region of helix 1 drawn in the right half, whereas the rest of protein is still denatured. At the bottom is the native structure with the lowest energy and entropy. The figure is based on ref. , and the protein structures pictured here were prepared with a graphics package, molmol (22).
See this image and copyright information in PMC

Comment on

References

    1. Fersht A R. Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding. New York: Freeman; 1999.
    1. Itzhaki L A, Otzen D E, Fersht A R. J Mol Biol. 1995;254:260–288. - PubMed
    1. Bryngelson J D, Onuchic J N, Socci N D, Wolynes P G. Proteins Struct Funct Genet. 1995;21:167–195. - PubMed
    1. Plaxco K W, Simons K T, Baker D. J Mol Biol. 1998;277:985–994. - PubMed
    1. Galzitskaya O V, Finkelstein A V. Proc Natl Acad Sci USA. 1999;96:11299–11304. - PMC - PubMed

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