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Article

Hydrophobic core flexibility modulates enzyme activity in HIV-1 protease.

Journal of the American Chemical Society - 7 Mar 2012

Mittal Seema, Cai Yufeng, Nalam Madhavi N L, Bolon Daniel N A, Schiffer Celia A

Abstract excerpt

Human immunodeficiency virus Type-1 (HIV-1) protease is crucial for viral maturation and infectivity. Studies of protease dynamics suggest that the rearrangement of the hydrophobic core is essential for enzyme activity. Many mutations in the hydrophobic core are also associated with drug resistance and may modulate the core flexibility. To test the role of flexibility in protease activity, pairs of cysteines were...

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Identifiers

PMID: 22295904
DOI: 10.1021/ja2095766
PMCID: PMC3391577

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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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