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Article

Structural studies of binding site tryptophan mutants in the high-affinity streptavidin-biotin complex.

Journal of molecular biology - 29 May 1998

Freitag S, Le Trong I, Chilkoti A, Klumb L A, Stayton P S, Stenkamp R E

Abstract excerpt

Previous thermodynamic and computational studies have pointed to the important energetic role of aromatic contacts in generating the exceptional binding free energy of streptavidin-biotin association. We report here the crystallographic characterization of single site tryptophan mutants in investigating structural consequences of alterations in these aromatic contacts. Four tryptophan residues, Trp79, Trp92,...

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Identifiers

PMID: 9636711
DOI: 10.1006/jmbi.1998.1735

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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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