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Volumn 44, Issue 45, 2005, Pages 14956-14968

Thermodynamics and kinetics of formation of the alkaline state of a Lys 79→Ala/Lys 73→His variant of iso-1-cytochrome c

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGEN BONDS; ISOMERIZATION; PERTURBATION TECHNIQUES; PH EFFECTS; PROTEINS; THERMODYNAMICS;

EID: 27744582890     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0515873     Document Type: Article
Times cited : (34)

References (56)
  • 2
    • 0015222174 scopus 로고
    • Studies on ferricytochrome c. 1. Effects of pH, ionic strength and protein denaturants on the spectra of ferricytochrome c
    • Greenwood, C., and Wilson, M. T. (1971) Studies on ferricytochrome c. 1. Effects of pH, ionic strength and protein denaturants on the spectra of ferricytochrome c, Eur. J. Biochem. 22, 5-10.
    • (1971) Eur. J. Biochem. , vol.22 , pp. 5-10
    • Greenwood, C.1    Wilson, M.T.2
  • 3
    • 0000431715 scopus 로고    scopus 로고
    • The alkaline transition in ferricytochrome c
    • (Scott, R. A., Mauk, A. G., Eds), University Science Books, Sausalito, CA
    • Wilson, M. T., and Greenwood, C. (1996) The alkaline transition in ferricytochrome c, in Cytochrome c: A Multidisciplinary Approach (Scott, R. A., Mauk, A. G., Eds) pp 611-634, University Science Books, Sausalito, CA.
    • (1996) Cytochrome c: A Multidisciplinary Approach , pp. 611-634
    • Wilson, M.T.1    Greenwood, C.2
  • 4
    • 0001370438 scopus 로고
    • Identification of Lys 79 as an iron ligand in one form of alkaline yeast iso-1-ferricytochrome c
    • Ferrer, J. C., Guillemette, T. G., Bogumil, R., Inglis, S. C., Smith, M. and Mauk, A. G. (1993) Identification of Lys 79 as an iron ligand in one form of alkaline yeast iso-1-ferricytochrome c, J. Am. Chem. Soc. 115, 7507-7508.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 7507-7508
    • Ferrer, J.C.1    Guillemette, T.G.2    Bogumil, R.3    Inglis, S.C.4    Smith, M.5    Mauk, A.G.6
  • 5
    • 0032508965 scopus 로고    scopus 로고
    • Proton-linked protein conformational switching: Definition of the alkaline conformational transition of yeast iso-1-ferricytochrome c
    • Rosell, F. I., Ferrer, J. C., and Mauk, A. G. (1998) Proton-linked protein conformational switching: Definition of the alkaline conformational transition of yeast iso-1-ferricytochrome c, J. Am. Chem. Soc. 120, 11234-11245.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11234-11245
    • Rosell, F.I.1    Ferrer, J.C.2    Mauk, A.G.3
  • 6
    • 0030614407 scopus 로고    scopus 로고
    • A lysine 73 → histidine variant of yeast iso-1-cytochrome c: Evidence for a native-like intermediate in the unfolding pathway and implications for m value effects
    • Godbole, S., Dong, A., Garbin, K., and Bowler, B. E. (1997) A lysine 73 → histidine variant of yeast iso-1-cytochrome c: Evidence for a native-like intermediate in the unfolding pathway and implications for m value effects, Biochemistry 36, 119-126.
    • (1997) Biochemistry , vol.36 , pp. 119-126
    • Godbole, S.1    Dong, A.2    Garbin, K.3    Bowler, B.E.4
  • 7
    • 0033524433 scopus 로고    scopus 로고
    • Effect of pH on formation of a nativelike intermediate on the unfolding pathway of a Lys 73 → His variant of yeast iso-1-cytochrome c
    • Godbole, S., and Bowler, B. E. (1999) Effect of pH on formation of a nativelike intermediate on the unfolding pathway of a Lys 73 → His variant of yeast iso-1-cytochrome c, Biochemistry 38, 487-495.
    • (1999) Biochemistry , vol.38 , pp. 487-495
    • Godbole, S.1    Bowler, B.E.2
  • 8
    • 0034619421 scopus 로고    scopus 로고
    • pH dependence of formation of a partially unfolded state of a Lys 73 → His variant of iso-1-cytochrome c: Implications for the alkaline conformational transition of cytochrome c
    • Nelson, C. J., and Bowler, B. E. (2000) pH dependence of formation of a partially unfolded state of a Lys 73 → His variant of iso-1-cytochrome c: Implications for the alkaline conformational transition of cytochrome c, Biochemistry 39, 13584- 13594.
    • (2000) Biochemistry , vol.39 , pp. 13584-13594
    • Nelson, C.J.1    Bowler, B.E.2
  • 9
    • 0034821575 scopus 로고    scopus 로고
    • Direct detection of heat and cold denaturation for partial unfolding of a protein
    • Nelson, C. J., LaConte, M. J., and Bowler, B. E. (2001) Direct detection of heat and cold denaturation for partial unfolding of a protein, J. Am. Chem. Soc. 123, 7453-7454.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 7453-7454
    • Nelson, C.J.1    Laconte, M.J.2    Bowler, B.E.3
  • 11
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai, Y., Sosnick, T. R., Mayne, L., and Englander, S. W. (1995) Protein folding intermediates: Native-state hydrogen exchange, Science 269, 192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 12
    • 0038786579 scopus 로고    scopus 로고
    • Cooperative omega loops in cytochrome c: Role in folding and function
    • Krishna, M. M. G., Lin, Y., Rumbley, J. N., and Englander, S. W. (2003) Cooperative omega loops in cytochrome c: Role in folding and function, J. Mol. Biol. 331, 29-36.
    • (2003) J. Mol. Biol. , vol.331 , pp. 29-36
    • Krishna, M.M.G.1    Lin, Y.2    Rumbley, J.N.3    Englander, S.W.4
  • 13
    • 0037126717 scopus 로고    scopus 로고
    • Chemically gated electron transfer: A means of accelerating and regulating rates of biological electron transfer
    • Davidson, V. L. (2002) Chemically gated electron transfer: A means of accelerating and regulating rates of biological electron transfer, Biochemistry 34, 14633-14636
    • (2002) Biochemistry , vol.34 , pp. 14633-14636
    • Davidson, V.L.1
  • 14
    • 0033975320 scopus 로고    scopus 로고
    • What controls rates of interprotein electron-transfer reactions?
    • Davidson, V. L. (2000) What controls rates of interprotein electron-transfer reactions?, Acc. Chem. Res. 33, 87-93.
    • (2000) Acc. Chem. Res. , vol.33 , pp. 87-93
    • Davidson, V.L.1
  • 15
    • 0001670167 scopus 로고
    • Evidence for the existence of two functionally distinct forms of cytochrome c monomer at alkaline pH
    • Greenwood, C., and Palmer, G. (1965) Evidence for the existence of two functionally distinct forms of cytochrome c monomer at alkaline pH, J. Biol. Chem. 240, 3660-3663.
    • (1965) J. Biol. Chem. , vol.240 , pp. 3660-3663
    • Greenwood, C.1    Palmer, G.2
  • 16
    • 0015222170 scopus 로고
    • Studies on ferricytochrome c. 2. A correlation between reducibility and the possession of the 695 nm absorption band of ferricytochrome c
    • Wilson, M. T., and Greenwood, C. (1971) Studies on ferricytochrome c. 2. A correlation between reducibility and the possession of the 695 nm absorption band of ferricytochrome c, Eur. J. Biochem. 22, 11-18.
    • (1971) Eur. J. Biochem. , vol.22 , pp. 11-18
    • Wilson, M.T.1    Greenwood, C.2
  • 18
    • 22144459030 scopus 로고    scopus 로고
    • Conformationally gated electron transfer in iso-1-cytochrome c: Engineering the rate of a conformational switch
    • Baddam, S., and Bowler, B. E. (2005) Conformationally gated electron transfer in iso-1-cytochrome c: Engineering the rate of a conformational switch, J. Am. Chem. Soc. 127, 9702-9703.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 9702-9703
    • Baddam, S.1    Bowler, B.E.2
  • 19
    • 0032508940 scopus 로고    scopus 로고
    • Alkaline conformational transition of ferricytochrome c studied by resonance Raman spectroscopy
    • Döpner, S., Hildebrant, P., Rosell, F. I., and Mauk, A. G. (1998) Alkaline conformational transition of ferricytochrome c studied by resonance Raman spectroscopy, J. Am. Chem. Soc. 120. 1126-11255.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 1126-11255
    • Döpner, S.1    Hildebrant, P.2    Rosell, F.I.3    Mauk, A.G.4
  • 20
    • 0033561331 scopus 로고    scopus 로고
    • The structural and functional role of lysine residues in the binding domain of cytochrome c in the electron transfer to cytochrome c oxidase
    • Döpner, S., Hildebrant, P., Rosell, F. I., Mauk, A. G., von Walter, M., Buse, G., and Soulimane, T. (1999) The structural and functional role of lysine residues in the binding domain of cytochrome c in the electron transfer to cytochrome c oxidase, Eur. J. Biochem. 261, 379-391.
    • (1999) Eur. J. Biochem. , vol.261 , pp. 379-391
    • Döpner, S.1    Hildebrant, P.2    Rosell, F.I.3    Mauk, A.G.4    Von Walter, M.5    Buse, G.6    Soulimane, T.7
  • 21
    • 2542585318 scopus 로고    scopus 로고
    • Proton-mediated dynamics of the alkaline conformational transition of yeast iso-1-cytochrome c
    • Martinez, R. E., and Bowler, B. E. (2004) Proton-mediated dynamics of the alkaline conformational transition of yeast iso-1-cytochrome c, J. Am. Chem. Soc. 126, 6751-6758.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 6751-6758
    • Martinez, R.E.1    Bowler, B.E.2
  • 22
    • 0026601458 scopus 로고
    • Site-directed mutagenesis of virtually any plasmid by eliminating a unique site
    • Deng, W. P. D., and Nickoloff, J. A. (1992) Site-directed mutagenesis of virtually any plasmid by eliminating a unique site, Anal. Biochem. 200, 81-88.
    • (1992) Anal. Biochem. , vol.200 , pp. 81-88
    • Deng, W.P.D.1    Nickoloff, J.A.2
  • 23
    • 0037031261 scopus 로고    scopus 로고
    • Effects of topology and excluded volume on protein denatured state conformational properties
    • Smith, C. R., Mateljevic, N., and Bowler, B. E. (2002) Effects of topology and excluded volume on protein denatured state conformational properties, Biochemistry 41, 10173-10181.
    • (2002) Biochemistry , vol.41 , pp. 10173-10181
    • Smith, C.R.1    Mateljevic, N.2    Bowler, B.E.3
  • 24
    • 0008556989 scopus 로고
    • Deletion mapping of sequences essential for the in vivo transcription of the iso-1-cytochrome c gene
    • Faye, G., Leung, D. W., Tatchell, K., Hall, B. D., and Smith, M. (1981) Deletion mapping of sequences essential for the in vivo transcription of the iso-1-cytochrome c gene. Proc. Natl. Acad. Sci. U.S.A. 78, 2258-2262.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 2258-2262
    • Faye, G.1    Leung, D.W.2    Tatchell, K.3    Hall, B.D.4    Smith, M.5
  • 25
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito H., Fukada, Y., Murata, K., and Kimura, A. (1983) Transformation of intact yeast cells treated with alkali cations, J. Bacteriol. 153, 163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukada, Y.2    Murata, K.3    Kimura, A.4
  • 26
    • 0035979801 scopus 로고    scopus 로고
    • Denatured state thermodynamics: Residual structure, chain stiffness and scaling factors
    • Hammack, B. N., Smith, C. R., and Bowler, B. E. (2001) Denatured state thermodynamics: Residual structure, chain stiffness and scaling factors, J. Mol. Biol. 311, 1091-1104.
    • (2001) J. Mol. Biol. , vol.311 , pp. 1091-1104
    • Hammack, B.N.1    Smith, C.R.2    Bowler, B.E.3
  • 27
    • 14344249796 scopus 로고    scopus 로고
    • Role of hydrogen bond networks and dynamics in positive and negative cooperative stabilization of a protein
    • Redzic, J. S., and Bowler, B. E. (2005) Role of hydrogen bond networks and dynamics in positive and negative cooperative stabilization of a protein, Biochemistry 44, 2900-2908.
    • (2005) Biochemistry , vol.44 , pp. 2900-2908
    • Redzic, J.S.1    Bowler, B.E.2
  • 28
    • 0027464611 scopus 로고
    • Destabilizing effects of replacing a surface lysine of cytochrome c with aromatic amino acids: Implications for the denatured state
    • Bowler, B. E., May, K., Zaragoza, T., York, P., Dong, A., and Caughey, W. S. (1993) Destabilizing effects of replacing a surface lysine of cytochrome c with aromatic amino acids: Implications for the denatured state, Biochemistry 32, 183-190.
    • (1993) Biochemistry , vol.32 , pp. 183-190
    • Bowler, B.E.1    May, K.2    Zaragoza, T.3    York, P.4    Dong, A.5    Caughey, W.S.6
  • 29
    • 0028287068 scopus 로고
    • Characterization of the guanidine hydrochloride-denatured state of iso-1-cytochrome c by infrared spectroscopy
    • Bowler, B. E., Dong, A., and Caughey, W. S. (1994) Characterization of the guanidine hydrochloride-denatured state of iso-1-cytochrome c by infrared spectroscopy, Biochemistry 33, 2402-2408.
    • (1994) Biochemistry , vol.33 , pp. 2402-2408
    • Bowler, B.E.1    Dong, A.2    Caughey, W.S.3
  • 30
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C. N. (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves, Methods Enzymol. 26, 266-280.
    • (1986) Methods Enzymol. , vol.26 , pp. 266-280
    • Pace, C.N.1
  • 31
    • 14044257270 scopus 로고    scopus 로고
    • Communication of stabilizing energy between substructures of a protein
    • Kristinsson, R., and Bowler, B. E. (2005) Communication of stabilizing energy between substructures of a protein, Biochemistry 44, 2349-2359.
    • (2005) Biochemistry , vol.44 , pp. 2349-2359
    • Kristinsson, R.1    Bowler, B.E.2
  • 32
    • 0017802519 scopus 로고
    • Solvent denaturation
    • Schellman, J. A. (1978) Solvent denaturation, Biopolymers 17, 1305-1322.
    • (1978) Biopolymers , vol.17 , pp. 1305-1322
    • Schellman, J.A.1
  • 34
    • 0037129949 scopus 로고    scopus 로고
    • Spectroscopic properties of a mitochondrial cytochrome c with a single thioether bond to the heme prosthetic group
    • Rosell, F. I., and Mauk, A. G. (2002) Spectroscopic properties of a mitochondrial cytochrome c with a single thioether bond to the heme prosthetic group, Biochemistry 41, 7811-7818.
    • (2002) Biochemistry , vol.41 , pp. 7811-7818
    • Rosell, F.I.1    Mauk, A.G.2
  • 35
    • 0034254338 scopus 로고    scopus 로고
    • Characterization of an alkaline transition intermediate stabilized in the Phe82Trp variant of yeast iso-1-cytochrome c
    • Rosell, F. I., Harris, T. R., Hildebrand, D. P., Döpner, S., Hildebrandt, P., and Mauk, A. G. (2000) Characterization of an alkaline transition intermediate stabilized in the Phe82Trp variant of yeast iso-1-cytochrome c, Biochemistry 39, 9047-9054.
    • (2000) Biochemistry , vol.39 , pp. 9047-9054
    • Rosell, F.I.1    Harris, T.R.2    Hildebrand, D.P.3    Döpner, S.4    Hildebrandt, P.5    Mauk, A.G.6
  • 36
    • 20544461199 scopus 로고    scopus 로고
    • Thermodynamics of protein interactions with urea and guanidinium hydrochloride
    • Makahatadze, G. I. (1999) Thermodynamics of protein interactions with urea and guanidinium hydrochloride, J. Phys Chem. B 103, 4781-4785.
    • (1999) J. Phys Chem. B , vol.103 , pp. 4781-4785
    • Makahatadze, G.I.1
  • 37
    • 0026754044 scopus 로고
    • A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range
    • Santoro, M. M., and Bolen, D. W. (1992) A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range, Biochemistry 31, 4901-4907.
    • (1992) Biochemistry , vol.31 , pp. 4901-4907
    • Santoro, M.M.1    Bolen, D.W.2
  • 38
    • 0026608669 scopus 로고
    • Oxidation state-dependent conformational changes in cytochrome c
    • Berghuis, A. M., and Brayer, G. D. (1992) Oxidation state-dependent conformational changes in cytochrome c, J. Mol. Biol. 223, 959-976.
    • (1992) J. Mol. Biol. , vol.223 , pp. 959-976
    • Berghuis, A.M.1    Brayer, G.D.2
  • 39
    • 0034635341 scopus 로고    scopus 로고
    • Measuring denatured state energetics: Deviations from random coil behavior and implications for the folding of iso-1-cytochrome c
    • Godbole, S., Hammack, B., and Bowler, B. E. (2000) Measuring denatured state energetics: Deviations from random coil behavior and implications for the folding of iso-1-cytochrome c, J. Mol. Biol. 296, 217-228.
    • (2000) J. Mol. Biol. , vol.296 , pp. 217-228
    • Godbole, S.1    Hammack, B.2    Bowler, B.E.3
  • 41
    • 0029039960 scopus 로고
    • Stabilizing amino acid replacements at position 52 in yeast iso-1-cytochromes c: In vivo and in vitro effects
    • Linske-O'Connell, L. I., Sherman, F., and McLendon, G. (1995) Stabilizing amino acid replacements at position 52 in yeast iso-1-cytochromes c: In vivo and in vitro effects, Biochemistry 34, 7094-7102.
    • (1995) Biochemistry , vol.34 , pp. 7094-7102
    • Linske-O'Connell, L.I.1    Sherman, F.2    McLendon, G.3
  • 42
    • 0042820062 scopus 로고    scopus 로고
    • Evaluation of cooperative interactions between substructures of iso-1-cytochrome c using double mutant cycles
    • Wandschneider, E., Hammack, B. N., and Bowler, B. E. (2003) Evaluation of cooperative interactions between substructures of iso-1-cytochrome c using double mutant cycles, Biochemistry 42, 10659-10666.
    • (2003) Biochemistry , vol.42 , pp. 10659-10666
    • Wandschneider, E.1    Hammack, B.N.2    Bowler, B.E.3
  • 43
    • 0028220311 scopus 로고
    • The role of a conserved internal water molecule and its associated hydrogen bond network in cytochrome c
    • Berghuis, A. M., Guillemette, J. G., McLendon, G., Sherman, F., Smith, M., and Brayer, G. D. (1994) The role of a conserved internal water molecule and its associated hydrogen bond network in cytochrome c, J. Mol. Biol. 236, 786-799.
    • (1994) J. Mol. Biol. , vol.236 , pp. 786-799
    • Berghuis, A.M.1    Guillemette, J.G.2    McLendon, G.3    Sherman, F.4    Smith, M.5    Brayer, G.D.6
  • 44
    • 0028300174 scopus 로고
    • Mutation of tyrosine-67 to phenylalanine in cytochrome c significantly alters the local heme environment
    • Berghuis, A. M., Guillemette, J. G., Smith, M., and Brayer, G. D. (1994) Mutation of tyrosine-67 to phenylalanine in cytochrome c significantly alters the local heme environment, J. Mol. Biol. 235, 1326-1341.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1326-1341
    • Berghuis, A.M.1    Guillemette, J.G.2    Smith, M.3    Brayer, G.D.4
  • 45
    • 0013660457 scopus 로고    scopus 로고
    • Nuclear magnetic resonance studies of class I cytochromes c
    • (Scott, R. A., Mauk, A. G., Eds.), University Science Books, Sausalito, CA
    • Pielak, G. J., Auld, D. S., Betz, S. F., Hilgen-Willis, S. E., and Garcia, L. L. (1996) Nuclear magnetic resonance studies of class I cytochromes c, in Cytochrome c: A Multidisciplinary Approach (Scott, R. A., Mauk, A. G., Eds.) pp 203-284, University Science Books, Sausalito, CA.
    • (1996) Cytochrome c: A Multidisciplinary Approach , pp. 203-284
    • Pielak, G.J.1    Auld, D.S.2    Betz, S.F.3    Hilgen-Willis, S.E.4    Garcia, L.L.5
  • 47
    • 0023762923 scopus 로고
    • Replacement of a conserved proline eliminates the absorbance-detected slow folding phase of iso-1-cytochrome c
    • Wood, L. C., White, T. B., Ramdas, L., and Nail, B. T. (1988) Replacement of a conserved proline eliminates the absorbance-detected slow folding phase of iso-1-cytochrome c, Biochemistry 27, 8563-8568.
    • (1988) Biochemistry , vol.27 , pp. 8563-8568
    • Wood, L.C.1    White, T.B.2    Ramdas, L.3    Nail, B.T.4
  • 48
    • 0030897736 scopus 로고    scopus 로고
    • Fast folding of cytochrome c
    • Pierce, M. M., and Nall, B. T. (1997) Fast folding of cytochrome c, Protein Sci. 6, 618-627.
    • (1997) Protein Sci. , vol.6 , pp. 618-627
    • Pierce, M.M.1    Nall, B.T.2
  • 49
    • 0037126686 scopus 로고    scopus 로고
    • Proline cis-trans isomerization and protein folding
    • Wedemeyer, W. J., Welker, E., Scheraga, H. A. (2002) Proline cis-trans isomerization and protein folding, Biochemistry 41, 14637-14644.
    • (2002) Biochemistry , vol.41 , pp. 14637-14644
    • Wedemeyer, W.J.1    Welker, E.2    Scheraga, H.A.3
  • 50
    • 0000247412 scopus 로고    scopus 로고
    • Proline isomerization and its catalysis in protein folding
    • (Pain, R. H., Ed.) 2nd ed., Oxford University Press, Inc., New York
    • Balbach, J., and Schmid, F. X. (2002) Proline isomerization and its catalysis in protein folding, in Mechanisms of Protein Folding (Pain, R. H., Ed.) 2nd ed., pp 212-249, Oxford University Press, Inc., New York.
    • (2002) Mechanisms of Protein Folding , pp. 212-249
    • Balbach, J.1    Schmid, F.X.2
  • 52
    • 0018556595 scopus 로고
    • Role of proline isomerization in the folding of ribonuclease a at low temperatures
    • Cook, K. H., Schmid, F. X., and Baldwin, R. L. (1979) Role of proline isomerization in the folding of ribonuclease A at low temperatures, Proc. Natl. Acad. Sci. U.S.A. 76, 6157-6161.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 6157-6161
    • Cook, K.H.1    Schmid, F.X.2    Baldwin, R.L.3
  • 53
    • 0019406826 scopus 로고
    • A native-like intermediate on the ribonuclease folding pathway. 2. Comparison of its properties to native ribonuclease a
    • Schmid, F. X., and Blaschek, H. (1981) A native-like intermediate on the ribonuclease folding pathway. 2. Comparison of its properties to native ribonuclease A, Eur. J. Biochem. 114, 111-117.
    • (1981) Eur. J. Biochem. , vol.114 , pp. 111-117
    • Schmid, F.X.1    Blaschek, H.2
  • 54
    • 0026648195 scopus 로고
    • Intramolecular catalysis of a proline isomerization reaction in the folding of dihydrofolate reductase
    • Texter, F. L., Spencer, D. B., Rosenstein, R., and Matthews, C. R. (1992) Intramolecular catalysis of a proline isomerization reaction in the folding of dihydrofolate reductase, Biochemistry 31, 5687-5691.
    • (1992) Biochemistry , vol.31 , pp. 5687-5691
    • Texter, F.L.1    Spencer, D.B.2    Rosenstein, R.3    Matthews, C.R.4
  • 56
    • 11844258838 scopus 로고    scopus 로고
    • EPR and optical spectroscopic studies of Met80X mutants of yeast ferricytochrome c. Models for intermediates in the alkaline transition
    • Silkstone, G. G., Cooper, C. E., Svistunenko, D., and Wilson, M. T. (2004) EPR and optical spectroscopic studies of Met80X mutants of yeast ferricytochrome c. Models for intermediates in the alkaline transition, J. Am. Chem. Soc. 127, 92-99.
    • (2004) J. Am. Chem. Soc. , vol.127 , pp. 92-99
    • Silkstone, G.G.1    Cooper, C.E.2    Svistunenko, D.3    Wilson, M.T.4


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