Study of protein-ligand binding by fluorescence

Biochemistry and Molecular Biology Education

Volumn 30, Issue 5, 2002, Pages 309-312

  Möller, Matías ^a   Denicola, Ana ^a  

^a UNIVERSIDAD DE LA REPÚBLICA   (Uruguay)

Author keywords

ANS; Binding sites for ANS in BSA; Effect of solvent polarity on fluorescence; Ligand binding; Scatchard

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ALBUMIN; ALCOHOL; AMPHOLYTE; LIGAND; MEMBRANE PROTEIN; TRYPTOPHAN;

AFFINITY LABELING; ARTICLE; BINDING SITE; COMPLEX FORMATION; DENATURATION; ENVIRONMENTAL CHANGE; EQUILIBRIUM CONSTANT; FLUORESCENCE ANALYSIS; HYDROPHOBICITY; LIGAND BINDING; MOLECULAR PROBE; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN FUNCTION; QUANTUM CHEMISTRY; STOICHIOMETRY;

EID: 33646151957     PISSN: 14708175     EISSN: None     Source Type: Journal    
DOI: 10.1002/bmb.2002.494030050089     Document Type: Article

References (16)

1. J. R. Lakowicz (1999) Principles of Fluorescence Spectroscopy, Kluwer Academic/Plenum Publishers, New York, pp. 1-24.
2. J. C. Croney, D. M. Jameson, R. P. Learmonth (2001) Fluorescence spectroscopy in biochemistry: teaching basic principles with visual demonstrations, Biochem. Mol. Biol. Educ. 29, 60-65.
3. K. E. van Holde, W. C. Johnson, P. S. Ho (1998) Principles of Physical Biochemistry, Prentice Hall, New Jersey, pp. 452-483.
4. I. D. Campbell, R. A. Dwek (1984) Biological Spectroscopy, The Benjamin/Cummings Publishing Co., Inc., Menlo Park, CA, pp. 97-98.
5. J. R. Lakowicz (1999) Principles of Fluorescence Spectroscopy, Kluer Academic/Plenum Publishers, New York, pp. 465-466.
6. L. Stryer (1968) Fluorescence spectroscopy of proteins, Science 162, 526-533.
7. M. Cardamone, N. K. Puri (1992) Spectrofluorimetric assessment of the surface hydrophobicity of proteins, Biochem. J. 282, 589-593.
8. I. Sirangelo, E. Bismuto, S. Tavassi, G. Irace (1998) Apomyoglobin folding intermediates characterized by the hydrophobic fluorescent probe 8-anilino-1-naphthalene sulfonate (ANS), Biochim. Biophys. Acta 1385, 69-77.
9. C. C. Chao, Y. S. Ma, E. R. Stadman (1997) Modification of protein surface hydrophobicity and methionine oxidation by oxidative systems, Proc. Natl. Acad. Sci. U. S. A. 94, 2969-2974.
10. E. Meucci, A. Mordente, G. E. Martorana (1991) Metal-catalized oxidation of human serum albumin: conformational and functional changes, J. Biol. Chem. 266, 4692-4699.
11. M. J. Davies, B. C. Gilbert, R. M. Haywood (1993) Radical-induced damage to bovine serum albumin: role of the cysteine residue, Free Radic. Res. Commun. 18, 353-367.
12. A. G. Gornall, C. J. Bardawill, M. M. David (1949) Determination of serum proteins by means of the biuret reaction, J. Biol. Chem. 177, 751-766.
13. K. E. van Holde, W. C. Johnson, P. S. Ho (1998) Principles of Physical Biochemistry, Prentice Hall, New Jersey, pp. 598-611.
14. N. C. Price, R. A. Dwek (1986) Principles and Problems in Physical Chemistry for Biochemists, 2nd ed., Oxford Science Publications, New York, pp. 221-223.
15. M. E. Georgiou, C. A. Georgiou, M. A. Koupparis (1999) Automated flow injection gradient technique for binding studies of micromolecules to proteins using potentiometric sensors: application to bovine serum albumin with anilinonaphthalenesulfonate probe and drugs, Anal. Chem. 71, 2541-2550.
16. M. Möller, A. Denicola (2002) Protein tryptophan accessibility studied by fluorescence quenching, Biochem. Mol. Biol. Educ. 30, 175-178.