Molecular Dynamics Studies on HIV-1 Protease: Drug Resistance and Folding Pathways

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dc.creatorCecconi, Fabio
dc.creatorMicheletti, Cristian
dc.creatorCarloni, Paolo
dc.creatorMaritan, Amos
dc.date2001-01-16
dc.date.accessioned2026-07-07T02:40:04Z
dc.date.available2026-07-07T02:40:04Z
dc.descriptionDrug resistance to HIV-1 Protease involves accumulation of multiple mutations in the protein. Here we investigate the role of these mutations by using molecular dynamics simulations which exploit the influence of the native-state topology in the folding process. Our calculations show that sites contributing to phenotypic resistance of FDA-approved drugs are among the most sensitive positions for the stability of partially folded states and should play a relevant role in the folding process. Furthermore, associations between amino acid sites mutating under drug treatment are shown to be statistically correlated. The striking correlation between clinical data and our calculations suggest a novel approach to the design of drugs tailored to bind regions crucial not only for protein function but also for folding.
dc.descriptionRevtex, 14 pages, 7 eps figures. Proteins, Structure Function and Genetics, in press (2001)
dc.identifierhttps://arxiv.org/abs/cond-mat/0101229
dc.identifierhttp://arxiv.org/abs/cond-mat/0101229
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/17257
dc.subjectStatistical Mechanics
dc.subjectSoft Condensed Matter
dc.subjectBiomolecules
dc.titleMolecular Dynamics Studies on HIV-1 Protease: Drug Resistance and Folding Pathways
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