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Article

The role of tryptophan in staphylococcal nuclease stability.

Biophysical chemistry - 1 Oct 2010

Hu Hong-Yu, Wu Ming-Chya, Fang Huey-Jen, Forrest Michael D, Hu Chin-Kun, Tsong Tian Yow, Chen Hueih Min

Abstract excerpt

Staphylococcal nuclease (SNase) has a single Trp residue at position 140. Circular dichroism, intrinsic and ANS-binding fluorescence, chemical titrations and enzymatic assays were used to measure the changes of its structure, stability and activities as the Trp was mutated or replaced to other positions. The results show that W140 is critical to SNase structure, stability, and function. Mutants such as W140A,...

Read the complete abstract on PubMed

Topics

Anilino Naphthalenesulfonates
Bromosuccinimide
Circular Dichroism
Enzyme Stability
Guanidine
Micrococcal Nuclease

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Models, Molecular

Mutagenesis, Site-Directed

Mutation

Protein Conformation

Protein Unfolding

Spectrometry, Fluorescence

Trifluoroethanol

Tryptophan

Source

Identifiers

PMID: 20688426
DOI: 10.1016/j.bpc.2010.07.001

Provenance

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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