Motion in Protein-like heteropolymer [plhp]

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Classification Complex Motion [C----]

Description The folding of a protein-like heteropolymer is studied by S Pande and DS Rokhsar. using direct simulation of a lattice model that folds rapidly to a well-defined ``native'' structure. By analysing the statistical properties of hundreds of folding events, they find folding ``pathway'' for such a polymer which includes partially folded, on-pathway intermediates that are shown to be metastable equilibrium states of the polymer. [Adapted from S Pande and DS Rokhsar, Folding pathway of a lattice model for protein folding]

Particular values describing motion Creation Date = 1999-07-28 21:43:48.000 Experimental Methods = m (molecular dynamics) Modification Date = 1999-07-28 21:47:33.000

References Zheng J; Knighton DR; Xuong NH; Taylor SS; Sowadski JM; Ten Eyck LF. Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations. Protein Science, 1993 Oct, 2(10):1559-73. [Medline info for 98132617] Zheng J; Knighton DR; Xuong NH; Taylor SS; Sowadski JM; Ten Eyck LF. Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations. Protein Science, 1993 Oct, 2(10):1559-73. [Medline info for 98179824] Zheng J; Knighton DR; Xuong NH; Taylor SS; Sowadski JM; Ten Eyck LF. Crystal structures of the myristylated catalytic subunit of cAMP-dependent protein kinase reveal open and closed conformations. Protein Science, 1993 Oct, 2(10):1559-73. [Medline info for 99145540]

Data and Graphics Protein Folding Papers Related Work of S Pande and DS Rokhsar. Folding pathway of a lattice model for protein folding Preprint of paper by same group

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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu