Modeling truncated hemoglobin vibrational dynamics

dc.creatorMarsella, Luca
dc.date2004-12-23
dc.date2005-04-25
dc.date.accessioned2026-07-07T03:02:55Z
dc.date.available2026-07-07T03:02:55Z
dc.descriptionWe present a study on the near equilibrium dynamics of two small proteins in the family of truncated hemoglobins, developed under the framework of a Gaussian network approach. Effective beta carbon atoms are taken into account besides C-alphas for all residues but glycines in the coarse-graining procedure, without leading to an increase in the degrees of freedom (betaGaussian Model). Normalized covariance matrix and deformation along slowest modes with collective character are analyzed, pointing out anti-correlations between functionally relevant sites for the proteins under study. In particular we underline the functional motions of an extended tunnel-cavity system running inside the protein matrix, which provide a pathway for small ligands binding with the iron in the heme group. We give a rough estimate of the order of magnitude of the relaxation times of the slowest two overdamped modes and compare results with previous studies on globins.
dc.description23 pages, 7 figures
dc.identifierhttps://arxiv.org/abs/cond-mat/0412661
dc.identifierhttp://arxiv.org/abs/cond-mat/0412661
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/25569
dc.subjectSoft Condensed Matter
dc.subjectBiomolecules
dc.titleModeling truncated hemoglobin vibrational dynamics
dc.typetext

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