Effect of temperature on tryptophan fluorescence of β-lactoglobulin B

This publication has 13 references indexed in Scilit:

• A conformational change in bovine β-lactoglobulin at low pH
  Biochimica et Biophysica Acta (BBA) - Protein Structure, 1975
• Solute perturbation of protein fluorescence. Quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion
  Biochemistry, 1971
• Thermodenaturation of bovine β-lactoglobulin
  Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971
• The denaturation of α-lactalbumin and β-lactoglobulin in heated milk
  Journal of Dairy Research, 1970
• The state of amino acid residues in β-lactoglobulin
  Archives of Biochemistry and Biophysics, 1969
• Heat Denaturation of Bovine β-Lactoglobulins and Relevance of Disulfide Aggregation
  Journal of Dairy Science, 1968
• Étude d'une étape réversible dans la thermodénaturation de la β-lactoglobuline bovine a
  Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis, 1965
• Comparison de la thermodénaturation des β-lactoglobulines A et B à pH 6.85
  Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis, 1965
• Heat Denaturation of β-Lactoglobulins A and B
  Journal of Dairy Science, 1962
• Solvent Effects in the Fluorescence of Indole and Substituted Indoles¹
  The Journal of Organic Chemistry, 1961