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Volumn 125, Issue 1, 2007, Pages 1-12

Photophysics of ANS. I. Protein-ANS complexes: Intestinal fatty acid binding protein and single-trp mutants

Author keywords

1,8 ANS; Exciton coupling; Non Foerster energy transfer

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; BINDING PROTEIN; INTESTINAL FATTY ACID BINDING PROTEIN; TRANSIENT RECEPTOR POTENTIAL CHANNEL; UNCLASSIFIED DRUG;

EID: 33750687239     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2006.07.016     Document Type: Article
Times cited : (13)

References (28)
  • 1
    • 0030070010 scopus 로고    scopus 로고
    • Characterization of the sources of protein-ligand affinity: 1-sulfonato-8-anilinonaphthalene binding to intestinal fatty acid binding protein
    • Kirk W., Kurian E., and Prendergast F. Characterization of the sources of protein-ligand affinity: 1-sulfonato-8-anilinonaphthalene binding to intestinal fatty acid binding protein. Biophys. J. 70 (1996) 69-83
    • (1996) Biophys. J. , vol.70 , pp. 69-83
    • Kirk, W.1    Kurian, E.2    Prendergast, F.3
  • 3
    • 33750735848 scopus 로고    scopus 로고
    • V. Likic, Structure and Dynamics of Internal Water In Rat Intestinal Fatty Acid Binding Protein Thesis, Mayo Graduate School of Medicine, Rochester, Minn, 1999.
  • 5
    • 0032787619 scopus 로고    scopus 로고
    • Structure and dynamics of the fatty acid binding cavity in apo rat intestinal fatty acid binding cavity
    • Likic V., and Prendergast F. Structure and dynamics of the fatty acid binding cavity in apo rat intestinal fatty acid binding cavity. Protein Sci. 8 (1999) 1649-1657
    • (1999) Protein Sci. , vol.8 , pp. 1649-1657
    • Likic, V.1    Prendergast, F.2
  • 6
    • 33750684447 scopus 로고    scopus 로고
    • E. Kurian, Solution Structure of Intestinal Fatty Acid Binding Protein complexed with 1-Anilinonaphthalene-8-sulfonate: Implications for Ligand Binding, Thesis, Mayo Graduate School of Medicine, Rochester Minn, 1998.
  • 7
    • 0016279769 scopus 로고
    • A rapid micromethod for the determination of nitrogen and phosphate in biological material
    • Jaenicke L. A rapid micromethod for the determination of nitrogen and phosphate in biological material. Anal. Biochem. 61 (1974) 623-627
    • (1974) Anal. Biochem. , vol.61 , pp. 623-627
    • Jaenicke, L.1
  • 8
    • 0029930226 scopus 로고    scopus 로고
    • Affinity of fatty acid for rRat intestinal fatty acid binding protein: further examination
    • Kurian E., Kirk W., and Prendergast F. Affinity of fatty acid for rRat intestinal fatty acid binding protein: further examination. Biochemistry 35 (1996) 3865-3874
    • (1996) Biochemistry , vol.35 , pp. 3865-3874
    • Kurian, E.1    Kirk, W.2    Prendergast, F.3
  • 9
    • 14744294498 scopus 로고    scopus 로고
    • The binding of 1,8 ANS congeners to I-FABP and comparison of some hypotheses about ANS' spectral sensitivity to environment
    • Kirk W.R. The binding of 1,8 ANS congeners to I-FABP and comparison of some hypotheses about ANS' spectral sensitivity to environment. Biochim. Biophys. Acta 1748 (2005) 84-93
    • (2005) Biochim. Biophys. Acta , vol.1748 , pp. 84-93
    • Kirk, W.R.1
  • 11
    • 0038131900 scopus 로고
    • Fluorescence spectroscopy data analysis environment: a second generation global analysis program
    • Beechem J.M., and Gratton E. Fluorescence spectroscopy data analysis environment: a second generation global analysis program. Proc. SPIE 909 (1988) 70-81
    • (1988) Proc. SPIE , vol.909 , pp. 70-81
    • Beechem, J.M.1    Gratton, E.2
  • 12
    • 0031150139 scopus 로고    scopus 로고
    • - 1 range and quantitative infrared spectroscopy of aqueous solutions
    • - 1 range and quantitative infrared spectroscopy of aqueous solutions. Anal. Biochem. 248 (1997) 234-245
    • (1997) Anal. Biochem. , vol.248 , pp. 234-245
    • Venyaminov, S.Y.1    Prendergast, F.2
  • 13
    • 0025693227 scopus 로고
    • 2O) solution. III. Estimation of the protein secondary structure
    • 2O) solution. III. Estimation of the protein secondary structure. Biopolymers 30 (1990) 1273-1280
    • (1990) Biopolymers , vol.30 , pp. 1273-1280
    • Kalnin, N.N.1    Baikalov, I.A.2    Venyaminov, S.3
  • 14
    • 0026712235 scopus 로고
    • Refinement of the structure of recombinant rat intestinal fatty acid-binding apoprotein at 1.2-Å resolution
    • Scapin G., Gordon J.I., and Sacchettini J.C. Refinement of the structure of recombinant rat intestinal fatty acid-binding apoprotein at 1.2-Å resolution. J. Biol. Chem. 267 (1992) 4253-4269
    • (1992) J. Biol. Chem. , vol.267 , pp. 4253-4269
    • Scapin, G.1    Gordon, J.I.2    Sacchettini, J.C.3
  • 15
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., and Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22 (1983) 2477-2637
    • (1983) Biopolymers , vol.22 , pp. 2477-2637
    • Kabsch, W.1    Sander, C.2
  • 16
    • 0031972919 scopus 로고    scopus 로고
    • 1-anilino-8-napthalene sulfonate anion-protein binding depends primarily on ion-pair formation
    • Matulis D., and Lovrien R. 1-anilino-8-napthalene sulfonate anion-protein binding depends primarily on ion-pair formation. Biophys. J. 74 (1998) 422-429
    • (1998) Biophys. J. , vol.74 , pp. 422-429
    • Matulis, D.1    Lovrien, R.2
  • 17
    • 0033135193 scopus 로고    scopus 로고
    • 1-anilino-8-naphthalene sulfonate as a protein conformational tightening agent
    • Matulis D., Baumann C., Bloomfield V., and Lovrien R. 1-anilino-8-naphthalene sulfonate as a protein conformational tightening agent. Bioplymers 49 (1999) 451-458
    • (1999) Bioplymers , vol.49 , pp. 451-458
    • Matulis, D.1    Baumann, C.2    Bloomfield, V.3    Lovrien, R.4
  • 18
    • 0032774245 scopus 로고    scopus 로고
    • Studies of the ligand binding reaction of adipocyte lipid binding protein using the fluorescent probe 1-anilinonaphthalene, 8-sulfonate
    • Ory J., and Banaszak L. Studies of the ligand binding reaction of adipocyte lipid binding protein using the fluorescent probe 1-anilinonaphthalene, 8-sulfonate. Biophys. J. 77 (1999) 1107-1116
    • (1999) Biophys. J. , vol.77 , pp. 1107-1116
    • Ory, J.1    Banaszak, L.2
  • 20
    • 0030610813 scopus 로고    scopus 로고
    • b transitions of tryptophan: applications of theory and experimental observations to fluorescence of proteins
    • b transitions of tryptophan: applications of theory and experimental observations to fluorescence of proteins. Methods Enzymol. 278 (1997) 113-150
    • (1997) Methods Enzymol. , vol.278 , pp. 113-150
    • Callis, P.1
  • 21
    • 0002413436 scopus 로고
    • Delocalized excitation and excitation transfer
    • Sinanoglu O. (Ed), Academic Pr. N.Y
    • Fœrster Th. Delocalized excitation and excitation transfer. In: Sinanoglu O. (Ed). Modern Quantum Chemistry (1964), Academic Pr. N.Y 93-137
    • (1964) Modern Quantum Chemistry , pp. 93-137
    • Fœrster, Th.1
  • 22
    • 33750702648 scopus 로고    scopus 로고
    • 0 significantly greater than the 60 μM we employ, but the possibility looms large that some quenching is contributed by nonspecifically bound ANS in another location on FABP.
  • 23
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher S.W., and Glockner J. Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20 (1981) 33-37
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glockner, J.2
  • 24
    • 0023656828 scopus 로고
    • Variable selection method improves the prediction of protein secondary structure from circular dichroism
    • Manavalan P., and Johnson Jr. W. Variable selection method improves the prediction of protein secondary structure from circular dichroism. Anal. Biochem. 167 (1987) 76-85
    • (1987) Anal. Biochem. , vol.167 , pp. 76-85
    • Manavalan, P.1    Johnson Jr., W.2
  • 25
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of the number of α-helical and β-strand segments in proteins using circular dichroism spectroscopy
    • Sreerama N., Yu.Venyaminov S., and Woody R.W. Estimation of the number of α-helical and β-strand segments in proteins using circular dichroism spectroscopy. Protein Sci. 8 (1999) 370-380
    • (1999) Protein Sci. , vol.8 , pp. 370-380
    • Sreerama, N.1    Yu.Venyaminov, S.2    Woody, R.W.3
  • 26
    • 0019871893 scopus 로고
    • Information content in the circular dichroism of proteins
    • Hennessey J.P., and Johnson Jr. W.C. Information content in the circular dichroism of proteins. Biochemistry 20 (1981) 1085-1094
    • (1981) Biochemistry , vol.20 , pp. 1085-1094
    • Hennessey, J.P.1    Johnson Jr., W.C.2
  • 28
    • 33750726871 scopus 로고    scopus 로고
    • - 1.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.