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Article

The folding free-energy surface of HIV-1 protease: insights into the thermodynamic basis for resistance to inhibitors.

Journal of molecular biology - 10 Apr 2009

Noel Amanda F, Bilsel Osman, Kundu Agnita, Wu Ying, Zitzewitz Jill A, Matthews C Robert

Abstract excerpt

Spontaneous mutations at numerous sites distant from the active site of human immunodeficiency virus type 1 protease enable resistance to inhibitors while retaining enzymatic activity. As a benchmark for probing the effects of these mutations on the conformational adaptability of this dimeric beta-barrel protein, the folding free-energy surface of a pseudo-wild-type variant, HIV-PR(*), was determined by a...

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Identifiers

PMID: 19150359
DOI: 10.1016/j.jmb.2008.12.061
PMCID: PMC2756696

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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