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Volumn 16, Issue 2, 2006, Pages 153-160

Time-resolved fluorescence studies on bovine serum albumin denaturation process

Author keywords

1 anilino 8 naphthalene sulfonate; Bovine serum albumin; Denaturation; Fluorescence lifetime distribution

Indexed keywords

1-ANILINO-8-NAPHTHALENE SULFONATE; BOVINE SERUM ALBUMIN; DENATURATION; FLUORESCENCE LIFETIME DISTRIBUTION;

EID: 33646698223     PISSN: 10530509     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10895-005-0029-9     Document Type: Conference Paper
Times cited : (40)

References (19)
  • 1
    • 0037686252 scopus 로고    scopus 로고
    • The present view of the mechanism of protein folding
    • V. Daggett and A. Fersht (2003). The present view of the mechanism of protein folding. Nature Reviews 4, 497-502.
    • (2003) Nature Reviews , vol.4 , pp. 497-502
    • Daggett, V.1    Fersht, A.2
  • 2
    • 0028856292 scopus 로고
    • Defective protein-folding as a basis of human-disease
    • P. J. Thomas, B.-H. Qu, and P. Pedersen (1995). Defective protein-folding as a basis of human-disease. Trends Biochem. Sci. 20, 456-459.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 456-459
    • Thomas, P.J.1    Qu, B.-H.2    Pedersen, P.3
  • 3
    • 0029918182 scopus 로고    scopus 로고
    • Misfolding the way to disease
    • G. Taubes (1996). Misfolding the way to disease. Science 271, 1493-1495.
    • (1996) Science , vol.271 , pp. 1493-1495
    • Taubes, G.1
  • 4
    • 0842281551 scopus 로고    scopus 로고
    • Principles of protein folding, misfolding and aggregation
    • C. M. Dobson (2004). Principles of protein folding, misfolding and aggregation. Seminar in Cell & Developmental Biology 15, 3-16.
    • (2004) Seminar in Cell & Developmental Biology , vol.15 , pp. 3-16
    • Dobson, C.M.1
  • 5
    • 0025856806 scopus 로고
    • Denatured states of proteins
    • K. A. Dill and D. Shortle (1991). Denatured states of proteins. Annu. Rev. Biochem. 60, 795-825.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 795-825
    • Dill, K.A.1    Shortle, D.2
  • 6
    • 0032989351 scopus 로고    scopus 로고
    • Observation of strange kinetics in protein folding
    • J. Sabelko, J. Ervin, and M. Gruebele (1999). Observation of strange kinetics in protein folding. Proc. Natl Acad. Sci. USA 96, 6031-6036.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 6031-6036
    • Sabelko, J.1    Ervin, J.2    Gruebele, M.3
  • 8
    • 0028558671 scopus 로고
    • Preliminary crystallographic studies of crystal forms of serum-albumin
    • D. C. Carter, B. Chang, J. X. Ho, K. Keeling, and Z. Krishnasami (1994). Preliminary crystallographic studies of crystal forms of serum-albumin. Eur. J. Biochem. 226, 1049-1052.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 1049-1052
    • Carter, D.C.1    Chang, B.2    Ho, J.X.3    Keeling, K.4    Krishnasami, Z.5
  • 9
    • 0028227096 scopus 로고
    • Structure of serum-albumin
    • D. C. Carter and J. X. Ho (1994). Structure of serum-albumin. Adv. Protein Chem. 45, 153-203.
    • (1994) Adv. Protein Chem. , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 10
    • 0026514355 scopus 로고
    • Spectrofluorimetric assessment of the surface hydrophobicity of proteins
    • M. Cardamone and N. K. Puri (1992). Spectrofluorimetric assessment of the surface hydrophobicity of proteins. Biochem. J. 282, 589-593.
    • (1992) Biochem. J. , vol.282 , pp. 589-593
    • Cardamone, M.1    Puri, N.K.2
  • 11
    • 0015490257 scopus 로고
    • Fluorescence probes for structure
    • L. Brand and J. R. Gohlke (1972). Fluorescence probes for structure. Annu. Rev. Biochem. 41, 843-868.
    • (1972) Annu. Rev. Biochem. , vol.41 , pp. 843-868
    • Brand, L.1    Gohlke, J.R.2
  • 12
    • 0021095677 scopus 로고
    • Intramolecular donor-acceptor systems .10. Multiple fluorescences from 8-(phenylamino)-1-naphthalenesulfonates
    • E. M. Kosower and H. Kanety (1983). Intramolecular donor-acceptor systems .10. Multiple fluorescences from 8-(phenylamino)-1-naphthalenesulfonates. J. Am. Chem. Soc. 105, 6236-6243.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 6236-6243
    • Kosower, E.M.1    Kanety, H.2
  • 13
    • 0033371033 scopus 로고    scopus 로고
    • Energy gap dependence of the nonradiative decay rate constant of 1-anilino-8-naphthalene sulfonate in reverse micelles
    • N. Kitamura, N. Sakata, H.-B. Kim, and S. Habuchi (1999). Energy gap dependence of the nonradiative decay rate constant of 1-anilino-8-naphthalene sulfonate in reverse micelles. Anal. Sci. 15, 413-419.
    • (1999) Anal. Sci. , vol.15 , pp. 413-419
    • Kitamura, N.1    Sakata, N.2    Kim, H.-B.3    Habuchi, S.4
  • 16
    • 0033049201 scopus 로고    scopus 로고
    • Evidence of heterogeneous 1-anilinonaphthalene-8-sulfonate binding to beta-lactoglobulin from fluorescence spectroscopy
    • L. D'Alfonso, M. Collini, and G. Baldini (1999). Evidence of heterogeneous 1-anilinonaphthalene-8-sulfonate binding to beta-lactoglobulin from fluorescence spectroscopy. Biochim. Biophys. Acta 1432, 194-202.
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 194-202
    • D'Alfonso, L.1    Collini, M.2    Baldini, G.3
  • 17
    • 0030579811 scopus 로고    scopus 로고
    • Use of fluorescence decay times of 8-ANS-protein complexes to study the conformational transitions in proteins which unfold through the molten globule state
    • V. N. Uversky, S. Winter, and G. Löber (1996). Use of fluorescence decay times of 8-ANS-protein complexes to study the conformational transitions in proteins which unfold through the molten globule state. Biophys. Chem. 60, 79-88.
    • (1996) Biophys. Chem. , vol.60 , pp. 79-88
    • Uversky, V.N.1    Winter, S.2    Löber, G.3
  • 19
    • 0030926943 scopus 로고    scopus 로고
    • Time-resolved fluorescence studies on site-directed mutants of human serum albumin
    • M. K. Helms, C. E. Petersen, N. V. Bhagavan, and D. M. Jameson (1997). Time-resolved fluorescence studies on site-directed mutants of human serum albumin. FEBES Lett. 408 67-70.
    • (1997) FEBES Lett. , vol.408 , pp. 67-70
    • Helms, M.K.1    Petersen, C.E.2    Bhagavan, N.V.3    Jameson, D.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.