Understanding the determinants of stability and folding of small globular proteins from their energetics

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dc.creatorTiana, G.
dc.creatorSimona, F.
dc.creatorDe Mori, G. M. S.
dc.creatorBroglia, R. A.
dc.creatorColombo, G.
dc.date2003-01-30
dc.date.accessioned2026-07-07T02:49:26Z
dc.date.available2026-07-07T02:49:26Z
dc.descriptionThe results of minimal model calculations suggest that the stability and the kinetic accessibility of the native state of small globular proteins are controlled by few "hot" sites. By mean of molecular dynamics simulations around the native conformation, which simulate the protein and the surrounding solvent at full--atom level, we generate an energetic map of the equilibrium state of the protein and simplify it with an Eigenvalue decomposition. The components of the Eigenvector associated with the lowest Eigenvalue indicate which are the "hot" sites responsible for the stability and for the fast folding of the protein. Comparison of these predictions with the results of mutatgenesis experiments, performed for five small proteins, provide an excellent agreement.
dc.identifierhttps://arxiv.org/abs/cond-mat/0301582
dc.identifierhttp://arxiv.org/abs/cond-mat/0301582
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/20792
dc.subjectSoft Condensed Matter
dc.subjectQuantitative Biology
dc.titleUnderstanding the determinants of stability and folding of small globular proteins from their energetics
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