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Article

Effects of temperature on the fluorescence intensity and anisotropy decays of staphylococcal nuclease and the less stable nuclease-conA-SG28 mutant.

Biochemistry - 17 Sept 1991

Eftink M R, Gryczynski I, Wiczk W, Laczko G, Lakowicz J R

Abstract excerpt

Frequency-domain fluorescence spectroscopy was used to investigate the effects of temperature on the intensity and anisotropy decays of the single tryptophan residues of Staphylococcal nuclease A and its nuclease-conA-SG28 mutant. This mutant has the beta-turn forming hexapeptide, Ser-Gly-Asn-Gly-Ser-Pro, substituted for the pentapeptide Tyr-Lys-Gly-Gln-Pro at positions 27-31. The intensity decays were analyzed...

Topics

Amino Acid Sequence
Enzyme Stability
Fluorescence Polarization
Micrococcal Nuclease
Molecular Sequence Data
Mutation
Protein Conformation
Temperature
Thermodynamics

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Identifiers

PMID: 1892812
DOI: 10.1021/bi00101a005
PMCID: PMC6897575

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1892812-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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