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Article

Hexamerization of the bacteriophage T4 capsid protein gp23 and its W13V mutant studied by time-resolved tryptophan fluorescence.

The journal of physical chemistry. B - 14 Dec 2006

Stortelder Aike, Hendriks Johnny, Buijs Joost B, Bulthuis Jaap, Gooijer Cees, van der Vies Saskia M, van der Zwan Gert

Abstract excerpt

The bacteriophage T4 capsid protein gp23 was studied using time-resolved and steady-state fluorescence of the intrinsic protein fluorophore tryptophan. In-vitro gp23 consists mostly of monomers at low temperature but forms hexamers at room temperature. To extend our knowledge of the structure and hexamerization characteristics of gp23, the temperature-dependent fluorescence properties of a tryptophan mutant...

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Identifiers

PMID: 17149929
DOI: 10.1021/jp064881t

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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