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

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

2001-01-16

arxiv.org/abs/cond-mat/0101229v1

Physics

Condensed Matter

Statistical Mechanics

Revtex, 14 pages, 7 eps figures. Proteins, Structure Function and Genetics, in press (2001)

Scientific paper

Drug 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.

Affiliated with

Also associated with

No associations

Rating

Molecular Dynamics Studies on HIV-1 Protease: Drug Resistance and Folding Pathways does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.

If you have personal experience with Molecular Dynamics Studies on HIV-1 Protease: Drug Resistance and Folding Pathways, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Molecular Dynamics Studies on HIV-1 Protease: Drug Resistance and Folding Pathways will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFWR-SCP-O-426451