Folding pathways of a helix-turn-helix model protein

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dc.creatorHoffmann, D.
dc.creatorKnapp, E. W.
dc.date1997-06-11
dc.date.accessioned2026-07-07T09:16:17Z
dc.date.available2026-07-07T09:16:17Z
dc.descriptionA small model polypeptide represented in atomic detail is folded using Monte Carlo dynamics. The polypeptide is designed to have a native conformation similar to the central part of the helix-turn-helix protein ROP. Starting from a beta-strand conformation or two different loop conformations of the protein glutamine synthetase, six trajectories are generated using the so-called window move in dihedral angle space. This move changes conformations locally and leads to realistic, quasi-continuously evolving trajectories. Four of the six trajectories end in stable native-like conformations. Their folding pathways show a fast initial development of a helix-bend-helix motif, followed by a dynamic behaviour predicted by the diffusion-collision model of Karplus and Weaver. The phenomenology of the pathways is consistent with experimental results.
dc.description24 pages, LaTeX, 6 figures, to appear in J. Phys. Chem., see also chem-ph/9602003
dc.identifierhttps://arxiv.org/abs/physics/9706018
dc.identifierhttp://arxiv.org/abs/physics/9706018
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/153303
dc.subjectBiological Physics
dc.subjectSoft Condensed Matter
dc.subjectChemical Physics
dc.subjectQuantitative Biology
dc.titleFolding pathways of a helix-turn-helix model protein
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