Environment of tryptophan residues in various conformational states of alpha-lactalbumin studied by time-resolved and steady-state fluorescence spectroscopy

Autor:	Alexander V. Ostrovsky, Victor I. Emelyanenko, Alexander V. Klimanov, Lina P. Kalinichenko, Eugene A. Permyakov
Rok vydání:	1988
Předmět:	Lactalbumin Chemistry Protein Conformation Organic Chemistry Biophysics Analytical chemistry Tryptophan Biochemistry Fluorescence Decay curve Red shift Crystallography Kinetics Spectrometry Fluorescence Tryptophan fluorescence Steady state fluorescence Animals Humans Cattle Magnesium ion
Zdroj:	Biophysical chemistry. 30(2)
ISSN:	0301-4622
Popis:	Decay curves for tryptophan fluorescence of bovine and human α-lactalbumin in different states (metal-free and Ca 2+ or Mg 2+ -loaded states of the native and thermally denatured proteins) have been measured at different wavelengths. The curves are best fitted by a sum of three exponents assigned to emission of individual tryptophan residues. The result suggests that the red shift of the fluorescence spectrum of α-lactalbumin caused by release of the bound Ca 2+ or thermal denaturation is due to changes in the environment of all emitting tryptophan residues.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1733f856eaa9912d0c0c200819ade615 https://pubmed.ncbi.nlm.nih.gov/3416039 Zobrazit plný text záznamu