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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 over...

Topics

Amino Acid Sequence
Aspartic Acid Endopeptidases
Binding Sites
Endopeptidases
Gene Products, pol
HIV Protease
HIV-1
Humans
Hydrogen Bonding
Molecular Sequence Data
Molecular Structure
Mutation
Pepsin A

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Renin

Thermodynamics

Source

Identifiers

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

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-2107098-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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