Contact Pair Dynamics During Folding of a Model Globular Protein, Hp-36

Simple item page
dc.creatorMukherjee, Arnab
dc.creatorBagchi, Biman
dc.date2002-12-16
dc.date.accessioned2026-07-07T02:48:46Z
dc.date.available2026-07-07T02:48:46Z
dc.descriptionThe dynamics of contact pair formation between various hydrophobic residues during folding of a model protein Hp-36 is investigated by Brownian dynamics simulation. Hydropathy scale and non-local helix propensity of amino acids are used to model the complex interaction potential. The resulting structure of the model protein mimics the native state of the real protein with a $RMSD$ of 4.5 Å. A contact pair distance time correlation function (CPCF), $C_{P}^{ij}(t)$, is introduced which shows multistage decay, including a {\it slow late stage dynamics} for a few specific pairs. {\it These pairs determine the long time folding rate}. Dynamics can be correlated with the landscape, relative contact order and topological contact.
dc.description4 pages including 4 figures. Submitted to the Phys. Rev. Lett
dc.identifierhttps://arxiv.org/abs/cond-mat/0212379
dc.identifierhttp://arxiv.org/abs/cond-mat/0212379
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/20533
dc.subjectSoft Condensed Matter
dc.subjectQuantitative Biology
dc.titleContact Pair Dynamics During Folding of a Model Globular Protein, Hp-36
dc.typetext

Files

Collections

arXiv