메뉴 건너뛰기




Volumn 9, Issue 1, 2000, Pages 158-169

A step toward the prediction of the fluorescence lifetimes of tryptophan residues in proteins based on structural and spectral data

Author keywords

Molecular dynamics simulations; Nonradiative rate constant; Protein dynamics; Radiative rate constant

Indexed keywords

CALCIUM BINDING PROTEIN; TRYPTOPHAN;

EID: 0343851580     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.1.158     Document Type: Article
Times cited : (40)

References (69)
  • 1
    • 0024294392 scopus 로고
    • Guanosine triphosphatase activating protein (GAP) interacts with the ras-p21 effector binding domain
    • Adari H, Lowy DR, Willumsen BM, Der CJ, McCormick F. 1988. Guanosine triphosphatase activating protein (GAP) interacts with the ras-p21 effector binding domain. Science 240:518-521.
    • (1988) Science , vol.240 , pp. 518-521
    • Adari, H.1    Lowy, D.R.2    Willumsen, B.M.3    Der, C.J.4    McCormick, F.5
  • 3
    • 0001163897 scopus 로고
    • Global resolution of heterogeneuos decay by phase modulation fluorometry: Mixtures and proteins
    • Beechem JM, Knutson JR, Ross JBA, Turner BW, Brand L. 1983. Global resolution of heterogeneuos decay by phase modulation fluorometry: Mixtures and proteins. Biochemistry 22:6054-6058.
    • (1983) Biochemistry , vol.22 , pp. 6054-6058
    • Beechem, J.M.1    Knutson, J.R.2    Ross, J.B.A.3    Turner, B.W.4    Brand, L.5
  • 5
    • 0002775934 scopus 로고
    • Interaction models for water in relation to protein hydratation
    • Pullman B, ed. Dordrecht: Reidel
    • Berendsen HJC, Postma JPM, Van Gunsteren WF, Hermans J. 1981. Interaction models for water in relation to protein hydratation. In: Pullman B, ed. Intramolecular forces. Dordrecht: Reidel. pp 331-342.
    • (1981) Intramolecular Forces , pp. 331-342
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Van Gunsteren, W.F.3    Hermans, J.4
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 0029850169 scopus 로고    scopus 로고
    • Log-normal description of fluorescence spectra of organic fluorophores
    • Burstein EA, Emelyanenko VI. 1996. Log-normal description of Fluorescence spectra of organic fluorophores. Photochem Photobiol 64:316-320.
    • (1996) Photochem Photobiol , vol.64 , pp. 316-320
    • Burstein, E.A.1    Emelyanenko, V.I.2
  • 11
    • 0031274669 scopus 로고    scopus 로고
    • Tryptophan fluorescence shifts in proteins from hybrid simulations: An electrostatic approach
    • Callis PR, Burgess BK. 1997. Tryptophan fluorescence shifts in proteins from hybrid simulations: An electrostatic approach. J Phys Chem 101:9429-9432.
    • (1997) J Phys Chem , vol.101 , pp. 9429-9432
    • Callis, P.R.1    Burgess, B.K.2
  • 12
    • 0017807890 scopus 로고
    • Construction and characterization of amplifiable multicopy DNA cloning vehicles from the P15a cryptic miniplasmid
    • Chang ACY, Cohen SN. 1978. Construction and characterization of amplifiable multicopy DNA cloning vehicles from the P15A cryptic miniplasmid. J Bacteriol 1:1141-1156.
    • (1978) J Bacteriol , vol.1 , pp. 1141-1156
    • Chang, A.C.Y.1    Cohen, S.N.2
  • 13
    • 0032516433 scopus 로고    scopus 로고
    • Toward understanding tryptophan fluorescence in proteins
    • Chen Y, Barkley MD. 1998. Toward understanding tryptophan fluorescence in proteins. Biochemistry 37:9976-9982
    • (1998) Biochemistry , vol.37 , pp. 9976-9982
    • Chen, Y.1    Barkley, M.D.2
  • 14
    • 0029904741 scopus 로고    scopus 로고
    • The peptide bond quenches indole fluorescence
    • Chen Y, Liu B, Yu H-T, Barkley MD. 1996. The peptide bond quenches indole fluorescence. J Am Chem Soc 11:9271-9278.
    • (1996) J Am Chem Soc , vol.11 , pp. 9271-9278
    • Chen, Y.1    Liu, B.2    Yu, H.-T.3    Barkley, M.D.4
  • 15
    • 0024656806 scopus 로고
    • Instrumental and analysis improvement in multifrequency phase fluorometry
    • Clays K, Jannes J, Engelborghs Y, Persoons A. 1989. Instrumental and analysis improvement in multifrequency phase fluorometry. J Phys E Sci Instrum 22:297-305.
    • (1989) J Phys E Sci Instrum , vol.22 , pp. 297-305
    • Clays, K.1    Jannes, J.2    Engelborghs, Y.3    Persoons, A.4
  • 16
    • 0033002410 scopus 로고    scopus 로고
    • Tryptophan rotamer distributions in amphipathic peptides at a lipid surface
    • Clayton AHA, Sawyer WH. 1999. Tryptophan rotamer distributions in amphipathic peptides at a lipid surface. Biophys J 76:3235-3242.
    • (1999) Biophys J , vol.76 , pp. 3235-3242
    • Clayton, A.H.A.1    Sawyer, W.H.2
  • 17
    • 0024297219 scopus 로고
    • Amino acid sequence of a sarcoplasmic calcium-binding protein from the sandworm nereis diversicolor
    • Collins JH, Cox JA, Theibert JL. 1988. Amino acid sequence of a sarcoplasmic calcium-binding protein from the sandworm Nereis diversicolor. J Biol Chem 263:15378-15385.
    • (1988) J Biol Chem , vol.263 , pp. 15378-15385
    • Collins, J.H.1    Cox, J.A.2    Theibert, J.L.3
  • 18
    • 0029167814 scopus 로고
    • Conformational heterogeneity of tryptophan in a protein crystal
    • Dahms TES, Willis KJ, Szabo AG. 1995. Conformational heterogeneity of tryptophan in a protein crystal. J Am Chem Soc 117:2321-2326.
    • (1995) J Am Chem Soc , vol.117 , pp. 2321-2326
    • Dahms, T.E.S.1    Willis, K.J.2    Szabo, A.G.3
  • 19
    • 0027950388 scopus 로고
    • Cloning, expression and purification of a sarcoplasmic calcium-binding protein from the sandworm nereis diversicolor via a fusion product with chloramphenicol acetyltransferase
    • Dekeyzer N, Engelborghs Y, Volckaert G. 1994. Cloning, expression and purification of a sarcoplasmic calcium-binding protein from the sandworm Nereis diversicolor via a fusion product with chloramphenicol acetyltransferase. Protein Eng 7:125-130.
    • (1994) Protein Eng , vol.7 , pp. 125-130
    • Dekeyzer, N.1    Engelborghs, Y.2    Volckaert, G.3
  • 20
    • 0023051513 scopus 로고
    • Study of the time-resolved tryptophan fluorescence of crystalline α-chymotrypsin
    • Desie G, Boens N, De Schryver FC. 1986. Study of the time-resolved tryptophan fluorescence of crystalline α-chymotrypsin. Biochemistry 25:8301-8308.
    • (1986) Biochemistry , vol.25 , pp. 8301-8308
    • Desie, G.1    Boens, N.2    De Schryver, F.C.3
  • 22
    • 0242618314 scopus 로고    scopus 로고
    • Calculation of pathways for the conformational transition between the GTP- and GDP-bound states of the Ha-ras-p21 protein: Calculations with explicit solvent simulations and comparison with calculations in vacuum
    • Díaz JF, Wroblowski B, Schlitter J, Engelborghs Y. 1997b. Calculation of pathways for the conformational transition between the GTP- and GDP-bound states of the Ha-ras-p21 protein: Calculations with explicit solvent simulations and comparison with calculations in vacuum. Proteins Struct Funct Genet 28:434-451.
    • (1997) Proteins Struct Funct Genet , vol.28 , pp. 434-451
    • Díaz, J.F.1    Wroblowski, B.2    Schlitter, J.3    Engelborghs, Y.4
  • 24
  • 25
    • 0025292625 scopus 로고
    • The photophysics of tryptophan in bacteriophage T4 lysozyme
    • Harris D, Hudson B. 1990. The photophysics of tryptophan in bacteriophage T4 lysozyme. Biochemistry 29:5276-5285.
    • (1990) Biochemistry , vol.29 , pp. 5276-5285
    • Harris, D.1    Hudson, B.2
  • 26
    • 36449005657 scopus 로고
    • Protein side chain rotational isomerisation: A minimum perturbation mapping study
    • Haydock C. 1993. Protein side chain rotational isomerisation: A minimum perturbation mapping study. J Chem Phys 95:8199-8214.
    • (1993) J Chem Phys , vol.95 , pp. 8199-8214
    • Haydock, C.1
  • 27
    • 0030982174 scopus 로고    scopus 로고
    • Quenching of the tryptophan fluorescence by the active-site disulfide bridge in the dsbA protein from Escherichia coli
    • Hennecke J. Sillen A, Huber-Wunderlich M, Engelborghs Y, Glockshuber R. 1997. Quenching of the tryptophan fluorescence by the active-site disulfide bridge in the dsbA protein from Escherichia coli. Biochemistry 36:6391-6400.
    • (1997) Biochemistry , vol.36 , pp. 6391-6400
    • Hennecke, J.1    Sillen, A.2    Huber-Wunderlich, M.3    Engelborghs, Y.4    Glockshuber, R.5
  • 28
    • 0032911428 scopus 로고    scopus 로고
    • An ionization/recombination mechanism for complexity of the fluorescence of tryptophan in proteins
    • Hudson BS. 1999. An ionization/recombination mechanism for complexity of the fluorescence of tryptophan in proteins. Acc Chem Res 32:297-300.
    • (1999) Acc Chem Res , vol.32 , pp. 297-300
    • Hudson, B.S.1
  • 29
    • 33947295202 scopus 로고
    • The influence of solvent and temperature upon the fluorescence of indole derivatives
    • Kirby EP, Steiner RFS. 1970. The influence of solvent and temperature upon the fluorescence of indole derivatives. J Phys Chem 74:4480-4490.
    • (1970) J Phys Chem , vol.74 , pp. 4480-4490
    • Kirby, E.P.1    Steiner, R.F.S.2
  • 30
    • 0026244229 scopus 로고
    • MOLSCRlPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. MOLSCRlPT: A program to produce both detailed and schematic plots of protein structures. J App Crystallogr 24:946-950.
    • (1991) J App Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 31
    • 0015919772 scopus 로고
    • Carp muscle calcium-binding protein. II. Structure determination and general description
    • Kretsinger RH, Nockolds CE. 1973. Carp muscle calcium-binding protein. II. Structure determination and general description. J Biol Chem 248: 119-174.
    • (1973) J Biol Chem , vol.248 , pp. 119-174
    • Kretsinger, R.H.1    Nockolds, C.E.2
  • 32
    • 0026124240 scopus 로고
    • SIMLYS - A software package for trajectory analysis of molecular dynamics simulations
    • Krüger P, Lüke M, Szameit A. 1991. SIMLYS - A software package for trajectory analysis of molecular dynamics simulations. Comput Phys Commun 62:371-380.
    • (1991) Comput Phys Commun , vol.62 , pp. 371-380
    • Krüger, P.1    Lüke, M.2    Szameit, A.3
  • 34
    • 0014675222 scopus 로고
    • Refinement of protein conformations using a macromolecular energy minimization procedure
    • Levitt M, Lifson S. 1969. Refinement of protein conformations using a macromolecular energy minimization procedure. J Mol Biol 46:269-279.
    • (1969) J Mol Biol , vol.46 , pp. 269-279
    • Levitt, M.1    Lifson, S.2
  • 35
    • 0026585599 scopus 로고
    • Statistical determination of the average values of the extinction coefficients of tryptophan and tyrosine in native proteins
    • Mach H, Middaugh CR, Lewis RV. 1992. Statistical determination of the average values of the extinction coefficients of tryptophan and tyrosine in native proteins. Anal Biochem 200:74-80.
    • (1992) Anal Biochem , vol.200 , pp. 74-80
    • Mach, H.1    Middaugh, C.R.2    Lewis, R.V.3
  • 36
    • 0022004980 scopus 로고
    • Electron transfer in chemistry and biology
    • Marcus RA, Sutin N. 1985. Electron transfer in chemistry and biology. Bioehim Biophys Acta 811:265-321.
    • (1985) Bioehim Biophys Acta , vol.811 , pp. 265-321
    • Marcus, R.A.1    Sutin, N.2
  • 37
    • 0023521842 scopus 로고
    • Analysis of the relationship between side-chain conformation and secondary structure in globular proteins
    • McGregor MJ, Suhail A, Sternberg MJE. 1987. Analysis of the relationship between side-chain conformation and secondary structure in globular proteins. J Mol Biol 198:295-310.
    • (1987) J Mol Biol , vol.198 , pp. 295-310
    • McGregor, M.J.1    Suhail, A.2    Sternberg, M.J.E.3
  • 38
    • 0001245416 scopus 로고
    • Fluoride complexes of beryllium (II) in aqueous media
    • Mesmer RE, Baes CF. 1969. Fluoride complexes of beryllium (II) in aqueous media. Inorg Chem 8:618-626.
    • (1969) Inorg Chem , vol.8 , pp. 618-626
    • Mesmer, R.E.1    Baes, C.F.2
  • 40
    • 0026027810 scopus 로고
    • Isolation and characterization of catalytic and calmodulin-binding domains of Bordetella pertussis adanylate cyclase
    • Munier H, Gilles A-M, Glaser P, Krin E, Danchin A, Sarfati R, Bàrzu O. 1991. Isolation and characterization of catalytic and calmodulin-binding domains of Bordetella pertussis adanylate cyclase. Eur J Biochem 196:469-474.
    • (1991) Eur J Biochem , vol.196 , pp. 469-474
    • Munier, H.1    Gilles, A.-M.2    Glaser, P.3    Krin, E.4    Danchin, A.5    Sarfati, R.6    Bàrzu, O.7
  • 41
    • 0025310575 scopus 로고
    • Refined crystal structure of the triphosphate conformation of H-ras-p21 at 1.35 å resolution: Implications for the mechanism of GTP hydrolysis
    • Pai EF, Krengel U, Petsko GA, Goody RS, Kabsh W, Wittinghofer A. 1990. Refined crystal structure of the triphosphate conformation of H-ras-p21 at 1.35 Å resolution: Implications for the mechanism of GTP hydrolysis. EMBO J 9:2351-2359.
    • (1990) EMBO J , vol.9 , pp. 2351-2359
    • Pai, E.F.1    Krengel, U.2    Petsko, G.A.3    Goody, R.S.4    Kabsh, W.5    Wittinghofer, A.6
  • 42
    • 33847682952 scopus 로고
    • Corrections of fluorescence spectra and the measurement of fluorescence quantum efficiency
    • Parker CA, Rees WT. 1960. Corrections of fluorescence spectra and the measurement of fluorescence quantum efficiency. Analyst 85:587-600.
    • (1960) Analyst , vol.85 , pp. 587-600
    • Parker, C.A.1    Rees, W.T.2
  • 44
    • 0028908679 scopus 로고
    • Substrate and product structural requirements for binding of nucleotides to H-ras p21: The mechanism of discrimination between guanosine and adenosine nucleotides
    • Rensland H, John J, Linke R, Simon I, Schlichting I, Wiltinghofer A, Goody RS. 1995. Substrate and product structural requirements for binding of nucleotides to H-ras p21: The mechanism of discrimination between guanosine and adenosine nucleotides. Biochemistry 34:593-599
    • (1995) Biochemistry , vol.34 , pp. 593-599
    • Rensland, H.1    John, J.2    Linke, R.3    Simon, I.4    Schlichting, I.5    Wiltinghofer, A.6    Goody, R.S.7
  • 45
    • 0019885903 scopus 로고
    • Time-resolved fluorescence of the two tryptophans in horse liver alcohol dehydrogenase
    • Ross JA, Schmid CJ, Brand L. 1981. Time-resolved fluorescence of the two tryptophans in horse liver alcohol dehydrogenase. Biochemistry 20:4369-4377.
    • (1981) Biochemistry , vol.20 , pp. 4369-4377
    • Ross, J.A.1    Schmid, C.J.2    Brand, L.3
  • 46
    • 33646940952 scopus 로고
    • Numerical integration of cartesian equations of motion of a system with constrains: Molecular dynamics of n-alkanes
    • Ryckaert JP, Ciccotti G, Berendsen HJC. 1977. Numerical integration of cartesian equations of motion of a system with constrains: Molecular dynamics of n-alkanes. J Comput Phys 23:327-341.
    • (1977) J Comput Phys , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 47
    • 0028455053 scopus 로고
    • Targeted molecular dynamics: A new approach for searching pathways of conformational transitions
    • Schlitter J, Engels M, Krüger P. 1994. Targeted molecular dynamics: A new approach for searching pathways of conformational transitions. J Mol Graphics 12:84-89.
    • (1994) J Mol Graphics , vol.12 , pp. 84-89
    • Schlitter, J.1    Engels, M.2    Krüger, P.3
  • 48
    • 0000821397 scopus 로고    scopus 로고
    • The correct use of "average" fluorescence parameters
    • Sillen A, Engelborghs Y. 1998. The correct use of "average" fluorescence parameters. Photochem Photobiol 67:475-486.
    • (1998) Photochem Photobiol , vol.67 , pp. 475-486
    • Sillen, A.1    Engelborghs, Y.2
  • 49
    • 0032738042 scopus 로고    scopus 로고
    • Fluorescence quenching in the dsba protein from escherichia coli. The complete picture of the excited state energy pathway and evidence for the reshuffling dynamics of the microstates of tryptophan
    • Sillen A, Hennecke J, Roethlisberger D, Glockshuber R, Engelborghs Y. 1999. Fluorescence quenching in the DsbA protein from Escherichia coli. The complete picture of the excited state energy pathway and evidence for the reshuffling dynamics of the microstates of tryptophan. Proteins Struct Funct Genet 37:253-263.
    • (1999) Proteins Struct Funct Genet , vol.37 , pp. 253-263
    • Sillen, A.1    Hennecke, J.2    Roethlisberger, D.3    Glockshuber, R.4    Engelborghs, Y.5
  • 50
    • 0030052607 scopus 로고    scopus 로고
    • Tryptophan dynamics of the FK506 binding protein: Time-resolved fluorescence and simulations
    • Silva ND, Prendergast FG. 1996. Tryptophan dynamics of the FK506 binding protein: Time-resolved fluorescence and simulations. Biophys J 70: 1122-1137.
    • (1996) Biophys J , vol.70 , pp. 1122-1137
    • Silva, N.D.1    Prendergast, F.G.2
  • 51
    • 36849126497 scopus 로고
    • Relationship between absorption intensity and fluorescence lifetime of molecules
    • Strickler SJ, Berg RA. 1962. Relationship between absorption intensity and fluorescence lifetime of molecules. J Chem Phys 37:814-822.
    • (1962) J Chem Phys , vol.37 , pp. 814-822
    • Strickler, S.J.1    Berg, R.A.2
  • 52
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier FW, Moffat BA. 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol 189:113-130.
    • (1986) J Mol Biol , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffat, B.A.2
  • 54
    • 0026473498 scopus 로고
    • Dilemma of correlating fluorescence quantum yields and intensity decay times in single tryptophan mutant proteins
    • Szabo AG, Faerman C. 1992. Dilemma of correlating fluorescence quantum yields and intensity decay times in single tryptophan mutant proteins. SPIE 1640:70-80.
    • (1992) SPIE , vol.1640 , pp. 70-80
    • Szabo, A.G.1    Faerman, C.2
  • 55
    • 0026086679 scopus 로고
    • Crystal structures at 2.2 å resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP
    • Tong LA, de Vos AM, Milburn MV, Kim SH. 1991. Crystal structures at 2.2 Å resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP. J Mol Biol 217:503-516.
    • (1991) J Mol Biol , vol.217 , pp. 503-516
    • Tong, L.A.1    De Vos, A.M.2    Milburn, M.V.3    Kim, S.H.4
  • 56
    • 0022727887 scopus 로고
    • Expression of p21 proteins in Escherichia coli and stereochemistry of then nucleotide-binding site
    • Tucker J, Sczakiel G, Feuerstein J, John J, Goody RS, Wittinghofer A. 1986. Expression of p21 proteins in Escherichia coli and stereochemistry of then nucleotide-binding site. EMBO J 5:1351-1358.
    • (1986) EMBO J , vol.5 , pp. 1351-1358
    • Tucker, J.1    Sczakiel, G.2    Feuerstein, J.3    John, J.4    Goody, R.S.5    Wittinghofer, A.6
  • 58
    • 0027234171 scopus 로고
    • Refolding and single-step purification of porcine interferon-gamma from escherichia coli inclusion bodies. Conditions for reconstitution of dimeric IFN-gamma
    • Vandenbroeck K, Martens E, D'Andrea S, Billiau A. 1993. Refolding and single-step purification of porcine interferon-gamma from Escherichia coli inclusion bodies. Conditions for reconstitution of dimeric IFN-gamma. Eur J Biochem 215:481-486.
    • (1993) Eur J Biochem , vol.215 , pp. 481-486
    • Vandenbroeck, K.1    Martens, E.2    D'Andrea, S.3    Billiau, A.4
  • 59
    • 0343666151 scopus 로고
    • Biomos Biomolecular Software b.v. Laboratory of Physical Chemistry University of Groningen
    • Van Gunsteren WF, Berendsen HJC. 1987. Program system GROMOS 87. Biomos Biomolecular Software b.v. Laboratory of Physical Chemistry University of Groningen.
    • (1987) Program System GROMOS 87
    • Van Gunsteren, W.F.1    Berendsen, H.J.C.2
  • 61
    • 0026545366 scopus 로고
    • Structure of a sarcoplasmic calcium-binding protein from Nereis diversicolor refined at 2.0 å resolution
    • Vijay-Kumar S, Cook WJ. 1992. Structure of a sarcoplasmic calcium-binding protein from Nereis diversicolor refined at 2.0 Å resolution. J Biol Chem 224:413-426.
    • (1992) J Biol Chem , vol.224 , pp. 413-426
    • Vijay-Kumar, S.1    Cook, W.J.2
  • 62
    • 0028465491 scopus 로고
    • A fluorescence study of tryptophan-histidine interaction in the peptide anantin and in solution
    • Vos R, Engelborghs Y. 1994. A fluorescence study of tryptophan-histidine interaction in the peptide anantin and in solution. Photochem Photobiol 60:24-32.
    • (1994) Photochem Photobiol , vol.60 , pp. 24-32
    • Vos, R.1    Engelborghs, Y.2
  • 63
    • 0031102343 scopus 로고    scopus 로고
    • Gigahertz phase fluorometry usina a fast high-gain photomultiplier
    • Vos R, Strobbe R, Engelborghs Y. 1997. Gigahertz phase fluorometry usina a fast high-gain photomultiplier. J Fluorescence 7:33S-35S.
    • (1997) J Fluorescence , vol.7
    • Vos, R.1    Strobbe, R.2    Engelborghs, Y.3
  • 64
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend G. 1990. WHAT IF: A molecular modeling and drug design program. J Mol Graphics 8:52-56.
    • (1990) J Mol Graphics , vol.8 , pp. 52-56
    • Vriend, G.1
  • 65
    • 0001142223 scopus 로고
    • Resolution of the fluorescence lifetimes in a heterogeneous system by phase and modulation measurements
    • Weber G. 1981. Resolution of the fluorescence lifetimes in a heterogeneous system by phase and modulation measurements. J Phys Chem 85:949-953.
    • (1981) J Phys Chem , vol.85 , pp. 949-953
    • Weber, G.1
  • 66
    • 0031313595 scopus 로고    scopus 로고
    • Intramolecular electron transfer between tryptophan radical and tyrosine in oligoproline-bridged model peptides and egg-white lysozyme
    • Wierzchowski KL. 1997. Intramolecular electron transfer between tryptophan radical and tyrosine in oligoproline-bridged model peptides and egg-white lysozyme. Acta Biochim Polon 44:627-644
    • (1997) Acta Biochim Polon , vol.44 , pp. 627-644
    • Wierzchowski, K.L.1
  • 67
    • 0028175552 scopus 로고
    • Probing α-helical secondary structure at a specific site in model peptides via restriction of tryptophan side-chain rotamer conformation
    • Willis KJ, Neugebauer W, Sikorska M, Szabo AG. 1994. Probing α-helical secondary structure at a specific site in model peptides via restriction of tryptophan side-chain rotamer conformation. Biophys J 66:1623-1630
    • (1994) Biophys J , vol.66 , pp. 1623-1630
    • Willis, K.J.1    Neugebauer, W.2    Sikorska, M.3    Szabo, A.G.4
  • 68
    • 0026701231 scopus 로고
    • Conformation of parathyroid hormone: Time-resolved fluorescence studies
    • Willis KJ, Szabo AG. 1992. Conformation of parathyroid hormone: Time-resolved fluorescence studies. Biochemistry 31:8924-8931.
    • (1992) Biochemistry , vol.31 , pp. 8924-8931
    • Willis, K.J.1    Szabo, A.G.2
  • 69
    • 0025740753 scopus 로고
    • The structure of ras protein: A model for a universal molecular switch
    • Wittinghofer A, Pai EF. 1991. The structure of ras protein: A model for a universal molecular switch. TIBS 16:382-387.
    • (1991) TIBS , vol.16 , pp. 382-387
    • Wittinghofer, A.1    Pai, E.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.