메뉴 건너뛰기




Volumn 318, Issue 2, 2003, Pages 300-308

Resolving near-ultraviolet circular dichroism spectra of single trp mutants in tear lipocalin

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS;

EID: 0038242826     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0003-2697(03)00215-X     Document Type: Article
Times cited : (11)

References (22)
  • 1
    • 0023226103 scopus 로고
    • Fluorescence properties of calmodulin-binding peptides reflect alpha-helical periodicity
    • O'Neil K.T., Wolfe H.R. Jr., Erickson-Viitanen S., DeGrado W.F. Fluorescence properties of calmodulin-binding peptides reflect alpha-helical periodicity. Science. 236:1987;1454-1456.
    • (1987) Science , vol.236 , pp. 1454-1456
    • O'Neil, K.T.1    Wolfe H.R., Jr.2    Erickson-Viitanen, S.3    DeGrado, W.F.4
  • 3
    • 0004040064 scopus 로고    scopus 로고
    • Principles of Fluorescence Spectroscopy
    • New York: Plenum Press
    • Lakowicz J.R. Principles of Fluorescence Spectroscopy. second ed. 1999;Plenum Press, New York.
    • (1999) second ed.
    • Lakowicz, J.R.1
  • 4
    • 0032516433 scopus 로고    scopus 로고
    • Toward understanding tryptophan fluorescence in proteins
    • Chen Y., Barkley M.D. Toward understanding tryptophan fluorescence in proteins. Biochemistry. 37:1998;9976-9982.
    • (1998) Biochemistry , vol.37 , pp. 9976-9982
    • Chen, Y.1    Barkley, M.D.2
  • 5
    • 0033964585 scopus 로고    scopus 로고
    • Trp scanning analysis of Tet repressor reveals conformational changes associated with operator and anhydrotetracycline binding
    • Kintrup M., Schubert P., Kunz M., Chabbert M., Alberti P., Bombarda E., Schneider S., Hillen W. Trp scanning analysis of Tet repressor reveals conformational changes associated with operator and anhydrotetracycline binding. Eur. J. Biochem. 267:2000;821-829.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 821-829
    • Kintrup, M.1    Schubert, P.2    Kunz, M.3    Chabbert, M.4    Alberti, P.5    Bombarda, E.6    Schneider, S.7    Hillen, W.8
  • 6
    • 0037032249 scopus 로고    scopus 로고
    • Fluorescence of cis-1-amino-2-(3-indolyl)cyclohexane-1-carboxylic acid: A single tryptophan chi(1) rotamer model
    • Liu B., Thalji R.K., Adams P.D., Fronczek F.R., McLaughlin M.L., Barkley M.D. Fluorescence of cis-1-amino-2-(3-indolyl)cyclohexane-1-carboxylic acid: a single tryptophan chi(1) rotamer model. J. Am. Chem. Soc. 124:2002;13329-13338.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 13329-13338
    • Liu, B.1    Thalji, R.K.2    Adams, P.D.3    Fronczek, F.R.4    McLaughlin, M.L.5    Barkley, M.D.6
  • 7
    • 0035846520 scopus 로고    scopus 로고
    • Site-directed tryptophan fluorescence reveals the solution structure of tear lipocalin: Evidence for freatures that confer promiscuity in ligand binding
    • Gasymov O.K., Abduragimov A.R., Yusifov T.N., Glasgow B.J. Site-directed tryptophan fluorescence reveals the solution structure of tear lipocalin: evidence for freatures that confer promiscuity in ligand binding. Biochemistry. 40:2001;14757-14762.
    • (2001) Biochemistry , vol.40 , pp. 14757-14762
    • Gasymov, O.K.1    Abduragimov, A.R.2    Yusifov, T.N.3    Glasgow, B.J.4
  • 8
    • 0015997959 scopus 로고
    • Aromatic contributions to circular dichroism spectra of proteins
    • Strickland E.H. Aromatic contributions to circular dichroism spectra of proteins. CRC Crit. Rev. Biochem. 2:1974;113-175.
    • (1974) CRC Crit. Rev. Biochem. , vol.2 , pp. 113-175
    • Strickland, E.H.1
  • 11
    • 0031274669 scopus 로고    scopus 로고
    • Tryptophan fluorescence shift in proteins from hybrid simulations: An electrostatic approach
    • Callis P.R., Burgess B.K. Tryptophan fluorescence shift in proteins from hybrid simulations: an electrostatic approach. J. Phys. Chem. B. 101:1997;9429-9432.
    • (1997) J. Phys. Chem. B , vol.101 , pp. 9429-9432
    • Callis, P.R.1    Burgess, B.K.2
  • 13
    • 0026726499 scopus 로고
    • CDNA cloning and sequencing reveals human tear prealbumin to be a member of the lipophilic-ligand carrier protein super family
    • Redl B., Holzfeind P., Lottspeich F. cDNA cloning and sequencing reveals human tear prealbumin to be a member of the lipophilic-ligand carrier protein super family. J. Biol. Chem. 267:1992;20282-20287.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20282-20287
    • Redl, B.1    Holzfeind, P.2    Lottspeich, F.3
  • 14
  • 15
    • 0033550079 scopus 로고    scopus 로고
    • Side chain mobility and ligand interactions of the G strand of tear lipocalins by site-directed spin labeling
    • Glasgow B.J., Gasymov O.K., Abduragimov A.R., Yusifov T.N., Altenbach C., Hubbell W.L. Side chain mobility and ligand interactions of the G strand of tear lipocalins by site-directed spin labeling. Biochemistry. 38:1999;13707-13716.
    • (1999) Biochemistry , vol.38 , pp. 13707-13716
    • Glasgow, B.J.1    Gasymov, O.K.2    Abduragimov, A.R.3    Yusifov, T.N.4    Altenbach, C.5    Hubbell, W.L.6
  • 16
    • 0015699132 scopus 로고
    • Oscillator strengths of the 1La and 1Lb absorption bands of tryptophan and several other indoles
    • Strickland E.H., Billups C. Oscillator strengths of the 1La and 1Lb absorption bands of tryptophan and several other indoles. Biopolymers. 12:1973;1989-1995.
    • (1973) Biopolymers , vol.12 , pp. 1989-1995
    • Strickland, E.H.1    Billups, C.2
  • 17
    • 0034003094 scopus 로고    scopus 로고
    • Resolution of ligand positions by site directed tryptophan fluorescence in tear lipocalin
    • Gasymov O.K., Abduragimov A.R., Yusifov T.N., Glasgow B.J. Resolution of ligand positions by site directed tryptophan fluorescence in tear lipocalin. Protein Sci. 9:2000;325-331.
    • (2000) Protein Sci. , vol.9 , pp. 325-331
    • Gasymov, O.K.1    Abduragimov, A.R.2    Yusifov, T.N.3    Glasgow, B.J.4
  • 19
    • 0037118710 scopus 로고    scopus 로고
    • RET and anisotropy measurements establish the proximity of the conserved Trp17 to Ile98 and Phe99 of tear lipocalin
    • Gasymov O.K., Abduragimov A.R., Yusifov T.N., Glasgow B.J. RET and anisotropy measurements establish the proximity of the conserved Trp17 to Ile98 and Phe99 of tear lipocalin. Biochemistry. 41:2002;8837-8848.
    • (2002) Biochemistry , vol.41 , pp. 8837-8848
    • Gasymov, O.K.1    Abduragimov, A.R.2    Yusifov, T.N.3    Glasgow, B.J.4
  • 21
    • 0015236372 scopus 로고
    • Near-ultraviolet absorption bands of tryptophan. Studies using horseradish peroxidase isoenzymes, bovine and horse heart cytochrome c, and N-stearyl-L-tryptophan n-hexyl ester
    • Strickland E.H., Horwitz J., Kay E., Shannon L.M., Wilchek M., Billups C. Near-ultraviolet absorption bands of tryptophan. Studies using horseradish peroxidase isoenzymes, bovine and horse heart cytochrome c, and N-stearyl-L-tryptophan n-hexyl ester. Biochemistry. 10:1971;2631-2638.
    • (1971) Biochemistry , vol.10 , pp. 2631-2638
    • Strickland, E.H.1    Horwitz, J.2    Kay, E.3    Shannon, L.M.4    Wilchek, M.5    Billups, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.