메뉴 건너뛰기




Volumn 39, Issue 10, 2010, Pages 1445-1451

Relationship between the wavelength maximum of a protein and the temperature dependence of its intrinsic tryptophan fluorescence intensity

Author keywords

Fluorescence; Free energy of unfolding; Post transition baseline; Pre transition baseline; Simulation

Indexed keywords

DRUG DERIVATIVE; N ACETYLTRYPTOPHAN; N-ACETYLTRYPTOPHANAMIDE; ORGANIC COMPOUND; PROTEIN; SOLVENT; TRYPTOPHAN; WATER;

EID: 77956178182     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-010-0601-3     Document Type: Article
Times cited : (11)

References (18)
  • 1
    • 0031808274 scopus 로고    scopus 로고
    • Baseline length and automated fitting of denaturation data
    • 10.1002/pro.5560070524 1:CAS:528:DyaK1cXivFKkurw%3D 9605334
    • DL Allen GJ Pielak 1998 Baseline length and automated fitting of denaturation data Protein Sci 7 1262 1263 10.1002/pro.5560070524 1:CAS:528:DyaK1cXivFKkurw%3D 9605334
    • (1998) Protein Sci , vol.7 , pp. 1262-1263
    • Allen, D.L.1    Pielak, G.J.2
  • 2
    • 0023442217 scopus 로고
    • Protein stability curves
    • 10.1002/bip.360261104 1:CAS:528:DyaL1cXntVykug%3D%3D 3689874
    • WJ Becktel JA Schellman 1987 Protein stability curves Biopolymers 26 1859 1877 10.1002/bip.360261104 1:CAS:528:DyaL1cXntVykug%3D%3D 3689874
    • (1987) Biopolymers , vol.26 , pp. 1859-1877
    • Becktel, W.J.1    Schellman, J.A.2
  • 3
    • 33847321948 scopus 로고    scopus 로고
    • Stability of globular proteins in H2O and D2O
    • 10.1002/bip.20645 1:CAS:528:DC%2BD2sXhvFWhs7g%3D 17143859
    • YM Efimova S Haemers B Wierczinski W Norde AA van Well 2007 Stability of globular proteins in H2O and D2O Biopolymers 85 264 273 10.1002/bip.20645 1:CAS:528:DC%2BD2sXhvFWhs7g%3D 17143859
    • (2007) Biopolymers , vol.85 , pp. 264-273
    • Efimova, Y.M.1    Haemers, S.2    Wierczinski, B.3    Norde, W.4    Van Well, A.A.5
  • 4
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • 10.1016/S0006-3495(94)80799-4 1:CAS:528:DyaK2cXivFegsbw%3D 8161701
    • MR Eftink 1994 The use of fluorescence methods to monitor unfolding transitions in proteins Biophys J 66 482 501 10.1016/S0006-3495(94)80799-4 1:CAS:528:DyaK2cXivFegsbw%3D 8161701
    • (1994) Biophys J , vol.66 , pp. 482-501
    • Eftink, M.R.1
  • 5
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor protein unfolding reactions
    • 10.1016/S0006-3495(94)80799-4
    • MR Eftink CY Wong 1994 The use of fluorescence methods to monitor protein unfolding reactions Biophys J 66 A164 A188 10.1016/S0006-3495(94)80799-4
    • (1994) Biophys J , vol.66
    • Eftink, M.R.1    Wong, C.Y.2
  • 6
    • 0028078606 scopus 로고
    • Estimation of the folding/unfolding energetics of marginally stable proteins using differential scanning calorimetry
    • 10.1006/abio.1994.1004 1:CAS:528:DyaK2cXnt1ynug%3D%3D 8135363
    • DT Haynie E Freire 1994 Estimation of the folding/unfolding energetics of marginally stable proteins using differential scanning calorimetry Anal Biochem 216 33 41 10.1006/abio.1994.1004 1:CAS:528:DyaK2cXnt1ynug%3D%3D 8135363
    • (1994) Anal Biochem , vol.216 , pp. 33-41
    • Haynie, D.T.1    Freire, E.2
  • 7
    • 33947295202 scopus 로고
    • The influence of solvent and temperature upon the fluorescence of indole derivative
    • 10.1021/j100720a004 1:CAS:528:DyaE3MXkslOnsw%3D%3D
    • EP Kirby EF Steiner 1970 The influence of solvent and temperature upon the fluorescence of indole derivative J Phys Chem 74 4480 4490 10.1021/j100720a004 1:CAS:528:DyaE3MXkslOnsw%3D%3D
    • (1970) J Phys Chem , vol.74 , pp. 4480-4490
    • Kirby, E.P.1    Steiner, E.F.2
  • 8
    • 0035545219 scopus 로고    scopus 로고
    • Thermodynamics of thermal denaturation of ribonuclease A and cytochrome c in the presence of 1,1,1,3,3,3-hexafluoro-2-propanol
    • 10.1006/jcht.2001.0844 1:CAS:528:DC%2BD3MXptFykt78%3D
    • N Kishore NK Ranjana 2001 Thermodynamics of thermal denaturation of ribonuclease A and cytochrome c in the presence of 1,1,1,3,3,3-hexafluoro-2- propanol J Chem Thermodyn 33 1325 1344 10.1006/jcht.2001.0844 1:CAS:528:DC%2BD3MXptFykt78%3D
    • (2001) J Chem Thermodyn , vol.33 , pp. 1325-1344
    • Kishore, N.1    Ranjana, N.K.2
  • 9
    • 0024498471 scopus 로고
    • A new method for determining the heat capacity change for protein folding
    • 10.1021/bi00432a026 1:CAS:528:DyaL1MXhtlWksbg%3D 2499351
    • CN Pace DV Laurents 1989 A new method for determining the heat capacity change for protein folding Biochemistry 28 2520 2525 10.1021/bi00432a026 1:CAS:528:DyaL1MXhtlWksbg%3D 2499351
    • (1989) Biochemistry , vol.28 , pp. 2520-2525
    • Pace, C.N.1    Laurents, D.V.2
  • 10
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • 10.1016/S0065-3233(08)60460-X 1:CAS:528:DyaL3cXhsF2jsr4%3D 44431
    • PL Privalov 1979 Stability of proteins: small globular proteins Adv Protein Chem 33 167 241 10.1016/S0065-3233(08)60460-X 1:CAS:528: DyaL3cXhsF2jsr4%3D 44431
    • (1979) Adv Protein Chem , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 11
    • 0024583245 scopus 로고
    • Thermodynamic problems of protein structure
    • 10.1146/annurev.bb.18.060189.000403 1:CAS:528:DyaL1MXktlGiurg%3D 2660833
    • PL Privalov 1989 Thermodynamic problems of protein structure Annu Rev Biophys Biophys Chem 18 47 69 10.1146/annurev.bb.18.060189.000403 1:CAS:528:DyaL1MXktlGiurg%3D 2660833
    • (1989) Annu Rev Biophys Biophys Chem , vol.18 , pp. 47-69
    • Privalov, P.L.1
  • 12
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: A calorimetric study
    • 10.1016/0022-2836(74)90188-0 1:CAS:528:DyaE2MXlt12gsA%3D%3D 4368360
    • PL Privalov NN Khechinashvili 1974 A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study J Mol Biol 86 665 684 10.1016/0022-2836(74)90188-0 1:CAS:528:DyaE2MXlt12gsA%3D%3D 4368360
    • (1974) J Mol Biol , vol.86 , pp. 665-684
    • Privalov, P.L.1    Khechinashvili, N.N.2
  • 13
    • 39649085800 scopus 로고    scopus 로고
    • Physical-chemical characterization and stability study of alpha-trypsin at pH 3.0 by differential scanning calorimetry
    • 10.1016/j.ijbiomac.2007.12.002 1:CAS:528:DC%2BD1cXitlOisL0%3D 18243299
    • AM Santos MA Santana FT Gomide AA Miranda JS Oliveira FA Boas AB Vasconcelos MP Bemquerer MM Santoro 2008 Physical-chemical characterization and stability study of alpha-trypsin at pH 3.0 by differential scanning calorimetry Int J Biol Macromol 42 278 284 10.1016/j.ijbiomac.2007.12.002 1:CAS:528:DC%2BD1cXitlOisL0%3D 18243299
    • (2008) Int J Biol Macromol , vol.42 , pp. 278-284
    • Santos, A.M.1    Santana, M.A.2    Gomide, F.T.3    Miranda, A.A.4    Oliveira, J.S.5    Boas, F.A.6    Vasconcelos, A.B.7    Bemquerer, M.P.8    Santoro, M.M.9
  • 14
    • 0023068366 scopus 로고
    • The thermodynamic stability of proteins
    • 10.1146/annurev.bb.16.060187.000555 1:CAS:528:DyaL2sXkvFWqu78%3D 3297085
    • JA Schellman 1987 The thermodynamic stability of proteins Annu Rev Biophys Biophys Chem 16 115 137 10.1146/annurev.bb.16.060187.000555 1:CAS:528:DyaL2sXkvFWqu78%3D 3297085
    • (1987) Annu Rev Biophys Biophys Chem , vol.16 , pp. 115-137
    • Schellman, J.A.1
  • 15
    • 0034141358 scopus 로고    scopus 로고
    • A possible origin of differences between calorimetric and equilibrium estimates of stability parameters of proteins
    • 10.1042/0264-6021:3450711 1:CAS:528:DC%2BD3cXisFOltL4%3D 10642532
    • A Sinha S Yadav R Ahmad F Ahmad 2000 A possible origin of differences between calorimetric and equilibrium estimates of stability parameters of proteins Biochem J 345 Pt 3 711 717 10.1042/0264-6021:3450711 1:CAS:528:DC%2BD3cXisFOltL4%3D 10642532
    • (2000) Biochem J , vol.345 , Issue.PART 3 , pp. 711-717
    • Sinha, A.1    Yadav, S.2    Ahmad, R.3    Ahmad, F.4
  • 16
    • 0026734102 scopus 로고
    • Two-dimensional differential scanning calorimetry: Simultaneous resolution of intrinsic protein structural energetics and ligand binding interactions by global linkage analysis
    • 10.1016/0003-2697(92)90311-T 1:CAS:528:DyaK38Xkt1arsbY%3D 1416022
    • M Straume E Freire 1992 Two-dimensional differential scanning calorimetry: simultaneous resolution of intrinsic protein structural energetics and ligand binding interactions by global linkage analysis Anal Biochem 203 259 268 10.1016/0003-2697(92)90311-T 1:CAS:528:DyaK38Xkt1arsbY%3D 1416022
    • (1992) Anal Biochem , vol.203 , pp. 259-268
    • Straume, M.1    Freire, E.2
  • 17
    • 0016368082 scopus 로고
    • Some applications of calorimetry in biochemistry and biology
    • 10.1146/annurev.bb.03.060174.000343 1:CAS:528:DyaE2cXls1Gls7g%3D 4370567
    • JM Sturtevant 1974 Some applications of calorimetry in biochemistry and biology Annu Rev Biophys Bioeng 3 35 51 10.1146/annurev.bb.03.060174.000343 1:CAS:528:DyaE2cXls1Gls7g%3D 4370567
    • (1974) Annu Rev Biophys Bioeng , vol.3 , pp. 35-51
    • Sturtevant, J.M.1
  • 18
    • 0026330844 scopus 로고
    • Calorimetric determination of the energetics of the molten globule intermediate in protein folding: Apo-alpha-lactalbumin
    • 10.1021/bi00108a010 1:CAS:528:DyaK3MXmt1Oks70%3D 1931986
    • D Xie V Bhakuni E Freire 1991 Calorimetric determination of the energetics of the molten globule intermediate in protein folding: apo-alpha-lactalbumin Biochemistry 30 10673 10678 10.1021/bi00108a010 1:CAS:528:DyaK3MXmt1Oks70%3D 1931986
    • (1991) Biochemistry , vol.30 , pp. 10673-10678
    • Xie, D.1    Bhakuni, V.2    Freire, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.