(Q68501878)

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

scientific article published on 01 June 1988

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24 September 2019

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

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24 September 2019

Environment of tryptophan residues in various conformational states of α-lactalbumin studied by time-resolved and steady-state fluorescence spectrosc (English)

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fluorescence spectroscopy

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organic chemistry

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A. V. Ostrovsky

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L. P. Kalinichenko

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V. I. Emelyanenko

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A. V. Klimanov

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9 January 2023

E. A. Permyakov

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1 June 1988

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Biophysical Chemistry

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24 September 2019

alpha-Lactalbumin: a calcium metalloprotein

2

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9 January 2023

Journal of Biological Chemistry

3

256

8582

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Kronman

publication date

1981

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9 January 2023

Metal ion binding to .alpha.-lactalbumin species

4

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Interactions of divalent metal ions with bovine, human, and goat alpha-lactalbumins

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Calcium binding to alpha-lactalbumin: structural rearrangement and association constant evaluation by means of intrinsic protein fluorescence changes

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alpha-Lactalbumin binds magnesium ions: study by means of intrinsic fluorescence technique

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Cation binding effects on the pH, thermal and urea denaturation transitions in alpha-lactalbumin

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Tryptophan fluorescence and homology in lysozymes and α-lactalbumins

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Time-resolved fluorescence from biological systems: tryptophan and simple peptides

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Time-resolved fluorescence of the two tryptophans in horse liver alcohol dehydrogenase.

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Decay-associated fluorescence spectra and the heterogeneous emission of alcohol dehydrogenase

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Acrylamide and oxygen fluorescence quenching studies with liver alcohol dehydrogenase using steady-state and phase fluorometry.

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Fluorescence Quenching and Energy Transfer in Complexes between Horse-Liver Alcohol Dehydrogenase and Coenzymes

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Conformational heterogeneity of the copper binding site in azurin. A time-resolved fluorescence study

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Biochimica et Biophysica Acta

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781

author name string

Permyakov

publication date

1985

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9 January 2023

Time-resolved fluorescence of proteins

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Journal of Biological Chemistry

24

250

3738

author name string

Formoso

publication date

1975

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A possible three-dimensional structure of bovine α-lactalbumin based on that of hen's egg-white lysozyme

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Computation of structures of homologous proteins. .alpha.-Lactalbumin from lysozyme

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Journal of Biological Chemistry

27

245

4570

author name string

Brew

publication date

1970

1 reference

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The Complete Amino-Acid Sequence of Human alpha-Lactalbumin

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Comparative fluorescence properties of bovine, goat, human and guinea pig alpha lactalbumin. Characterization of the environments of individual tryptophan residues in partially folded conformers

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Equilibrium and kinetics of the thermal unfolding of α-lactalbumin. The relation to its folding mechanism

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Luminescence of phenylalanine residues in superoxide dismutase from green pea

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Ultraviolet fluorescence of the aromatic amino acids

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On the analysis of fluorescence decay kinetics by the method of least-squares

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Structural elucidation of a hydrophobic box in bovine alpha-lactalbumin by NMR: nuclear Overhauser effects.

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10.1016/0301-4622(88)85008-7

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24 September 2019

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24 September 2019

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