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Article

Modulation of the affinity of aspartic proteases by the mutated residues in active site models.

FEBS letters - 26 Feb 1990

Goldblum A

Abstract excerpt

The active sites of 3 types of aspartic proteases are modeled, based on crystallographic coordinates of endothiapepsin and of a model of HIV-1 protease. The enthalpies of deprotonation from neutral to mono-anion and to dianion are calculated with semiempirical minimal neglect of differential overlap, hydrogen bonding corrected (MNDO/H). This quantum mechanical study of models for the active sites of pepsins,...

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Identifiers

PMID: 2107098
DOI: 10.1016/0014-5793(90)80562-w

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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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