메뉴 건너뛰기




Volumn 44, Issue 8, 2005, Pages 2900-2908

Role of hydrogen bond networks and dynamics in positive and negative cooperative stabilization of a protein

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; GENETIC ENGINEERING; HYDROGEN BONDS; MUTAGENESIS; THERMODYNAMICS; YEAST;

EID: 14344249796     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048218b     Document Type: Article
Times cited : (34)

References (33)
  • 1
    • 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
  • 2
    • 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
  • 4
    • 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
  • 5
    • 10544228949 scopus 로고    scopus 로고
    • The role of a conserved water molecule in the redox-dependent thermal stability of iso-1-cytochrome c
    • Lett, C. M., Berghuis, A. M., Frey, H. E., Lepock, J. R., and Guillemette, J. G. (1996) The role of a conserved water molecule in the redox-dependent thermal stability of iso-1-cytochrome c, J. Biol. Chem. 271, 29088-29093.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29088-29093
    • Lett, C.M.1    Berghuis, A.M.2    Frey, H.E.3    Lepock, J.R.4    Guillemette, J.G.5
  • 6
    • 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
  • 7
    • 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
  • 8
    • 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
  • 9
    • 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
  • 10
    • 0035923433 scopus 로고    scopus 로고
    • Energetics of side chain packing in staphylococcal nuclease assessed by systematic double mutant cycles
    • Chen, J., and Stites, W. E. (2001) Energetics of side chain packing in staphylococcal nuclease assessed by systematic double mutant cycles, Biochemistry 40, 14004-14011.
    • (2001) Biochemistry , vol.40 , pp. 14004-14011
    • Chen, J.1    Stites, W.E.2
  • 11
    • 0035923416 scopus 로고    scopus 로고
    • Higher-order packing interactions in triple and quadruple mutants of staphylococcal nuclease
    • Chen, J., and Stites, W. E. (2001) Higher-order packing interactions in triple and quadruple mutants of staphylococcal nuclease, Biochemistry 40, 14012-14019.
    • (2001) Biochemistry , vol.40 , pp. 14012-14019
    • Chen, J.1    Stites, W.E.2
  • 12
    • 0026587310 scopus 로고
    • Cooperative interactions during protein folding
    • Horovitz, A., and Fersht, A. R. (1992) Cooperative interactions during protein folding, J. Mol. Biol. 224, 733-740.
    • (1992) J. Mol. Biol. , vol.224 , pp. 733-740
    • Horovitz, A.1    Fersht, A.R.2
  • 13
    • 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
  • 14
    • 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
  • 15
    • 0026601458 scopus 로고
    • Site-directed mutagenesis on virtually any plasmid by eliminating a unique restriction site
    • Deng, W. P. D., and Nickoloff, J. A. (1992) Site-directed mutagenesis on virtually any plasmid by eliminating a unique restriction site, Anal. Biochem. 200, 81-88.
    • (1992) Anal. Biochem. , vol.200 , pp. 81-88
    • Deng, W.P.D.1    Nickoloff, J.A.2
  • 16
    • 0002038533 scopus 로고    scopus 로고
    • Site-directed replacement of the invariant lysine 73 of Saccharomyces cerevisiae iso-1-cytochrome c with all ribosomally encoded amino acids
    • Herrmann, L., Flatt, P., and Bowler, B. E. (1996) Site-directed replacement of the invariant lysine 73 of Saccharomyces cerevisiae iso-1-cytochrome c with all ribosomally encoded amino acids, Inorg. Chim. Acta 242, 97-103.
    • (1996) Inorg. Chim. Acta , vol.242 , pp. 97-103
    • Herrmann, L.1    Flatt, P.2    Bowler, B.E.3
  • 17
    • 0032488914 scopus 로고    scopus 로고
    • Cytochrome c folding traps are not due solely to histidine-heme ligation: Direct demonstration of a role for N-terminal amino group-heme Iigation
    • Hammack, B., Godbole, S., and Bowler, B. E. (1998) Cytochrome c folding traps are not due solely to histidine-heme ligation: Direct demonstration of a role for N-terminal amino group-heme Iigation, J. Mol. Biol. 275, 719-724.
    • (1998) J. Mol. Biol. , vol.275 , pp. 719-724
    • Hammack, B.1    Godbole, S.2    Bowler, B.E.3
  • 18
    • 0027383834 scopus 로고
    • Patterns of nonadditivity between pairs of stability mutations in Staphylococcal nuclease
    • Green, S. M., and Shortle, D. (1993) Patterns of nonadditivity between pairs of stability mutations in Staphylococcal nuclease, Biochemistry 32, 10131-10139.
    • (1993) Biochemistry , vol.32 , pp. 10131-10139
    • Green, S.M.1    Shortle, D.2
  • 19
    • 2442498470 scopus 로고    scopus 로고
    • On evolutionary conservation of thermodynamic coupling in proteins
    • Aldrich, R. W., and Fodor, A. A. (2004) On evolutionary conservation of thermodynamic coupling in proteins, J. Biol. Chem. 279, 19046-19050.
    • (2004) J. Biol. Chem. , vol.279 , pp. 19046-19050
    • Aldrich, R.W.1    Fodor, A.A.2
  • 20
    • 0347719392 scopus 로고    scopus 로고
    • Local complexity of amino acid interactions in a protein core
    • Jain, R. K., and Ranganathan, R. (2004) Local complexity of amino acid interactions in a protein core. Proc. Natl. Acad. Sci. U.S.A. 101, 111-116.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 111-116
    • Jain, R.K.1    Ranganathan, R.2
  • 21
    • 0029785464 scopus 로고    scopus 로고
    • Potential use of additivity of mutational effects in simplifying protein engineering
    • Skinner, M. M., and Terwilliger, T. C. (1996) Potential use of additivity of mutational effects in simplifying protein engineering. Proc. Natl. Acad. Sci. U.S.A. 93, 10753-10757.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 10753-10757
    • Skinner, M.M.1    Terwilliger, T.C.2
  • 22
    • 0023668221 scopus 로고
    • Temperature-sensitive mutations of bacteriophage T4 lysozyme occur at sites with low mobility and low solvent accessibility in the folded protein
    • Alber, T., Dao-pin, S., Nye, J. A., Muchmore, D. C., and Matthews, B. W. (1987) Temperature-sensitive mutations of bacteriophage T4 lysozyme occur at sites with low mobility and low solvent accessibility in the folded protein, Biochemistry 26, 3754-3758.
    • (1987) Biochemistry , vol.26 , pp. 3754-3758
    • Alber, T.1    Dao-pin, S.2    Nye, J.A.3    Muchmore, D.C.4    Matthews, B.W.5
  • 23
    • 0020825328 scopus 로고
    • The conformation of eukaryotic cytochrome c around residues 39, 57, 59, and 74
    • Robinson, M. N., Boswell, A. P., Huang, Z. X., Eley, C. G. S., and Moore, G. R. (1983) The conformation of eukaryotic cytochrome c around residues 39, 57, 59, and 74, Biochem. J. 213, 687-700.
    • (1983) Biochem. J. , vol.213 , pp. 687-700
    • Robinson, M.N.1    Boswell, A.P.2    Huang, Z.X.3    Eley, C.G.S.4    Moore, G.R.5
  • 24
    • 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
  • 25
    • 0030967237 scopus 로고    scopus 로고
    • Thermal denaturation of iso-1-cytochrome c variants: Comparison with solvent denaturation
    • Herrmann, L. M., and Bowler, B. E. (1997) Thermal denaturation of iso-1-cytochrome c variants: Comparison with solvent denaturation, Protein Sci. 6, 657-665.
    • (1997) Protein Sci. , vol.6 , pp. 657-665
    • Herrmann, L.M.1    Bowler, B.E.2
  • 26
    • 0027935843 scopus 로고
    • Stability of yeast iso-1-cytochrome c as a function of pH and temperature
    • Cohen, D. S., and Pielak, G. J. (1994) Stability of yeast iso-1-cytochrome c as a function of pH and temperature, Protein Sci. 3, 1253-1260.
    • (1994) Protein Sci. , vol.3 , pp. 1253-1260
    • Cohen, D.S.1    Pielak, G.J.2
  • 27
    • 0027000943 scopus 로고
    • Introduction of a disulfide bond in cytochrome c stabilizes a compact denatured state
    • Betz, S. F., and Pielak, G. J. (1992) Introduction of a disulfide bond in cytochrome c stabilizes a compact denatured state, Biochemistry 31, 12337-12344.
    • (1992) Biochemistry , vol.31 , pp. 12337-12344
    • Betz, S.F.1    Pielak, G.J.2
  • 28
    • 0030748706 scopus 로고    scopus 로고
    • Solution structure of oxidized Saccharomyces cerevisiae iso-1-cytochrome c
    • Banci, L., Bertini, I., Bren, K. L., Gray, H. B., Sompornpisut, P., and Turano, P. (1997) Solution structure of oxidized Saccharomyces cerevisiae iso-1-cytochrome c, Biochemistry 36, 8992-9001.
    • (1997) Biochemistry , vol.36 , pp. 8992-9001
    • Banci, L.1    Bertini, I.2    Bren, K.L.3    Gray, H.B.4    Sompornpisut, P.5    Turano, P.6
  • 29
    • 0031955820 scopus 로고    scopus 로고
    • Mutagenesis of histidine 26 demonstrates the importance of loop-loop and loop-protein interactions for the function of iso-1-cytochrome c
    • Fetrow, J. S., Dreher, U., Wiland, D. J., Schaak, D. L., and Boose, T. L. (1998) Mutagenesis of histidine 26 demonstrates the importance of loop-loop and loop-protein interactions for the function of iso-1-cytochrome c, Protein Sci. 7, 994-1005.
    • (1998) Protein Sci. , vol.7 , pp. 994-1005
    • Fetrow, J.S.1    Dreher, U.2    Wiland, D.J.3    Schaak, D.L.4    Boose, T.L.5
  • 31
    • 0033528743 scopus 로고    scopus 로고
    • 15N]-labeled oxidized and reduced iso-1-cytochrome c
    • 15N]-labeled oxidized and reduced iso-1-cytochrome c, Biochemistry 38, 4493-4503.
    • (1999) Biochemistry , vol.38 , pp. 4493-4503
    • Baxter, S.M.1    Fetrow, J.S.2
  • 32
    • 0031745764 scopus 로고    scopus 로고
    • Site-specific analysis of mutational effects in proteins
    • Di Cera, E. (1998) Site-specific analysis of mutational effects in proteins, Adv. Protein Chem. 51, 59-119.
    • (1998) Adv. Protein Chem. , vol.51 , pp. 59-119
    • Di Cera, E.1
  • 33
    • 2342544028 scopus 로고    scopus 로고
    • Conformational properties of the iso-1-cytochrome c denatured state: Dependence on guanidine hydrochloride concentration
    • Wandschneider, E., and Bowler, B. E. (2004) Conformational properties of the iso-1-cytochrome c denatured state: Dependence on guanidine hydrochloride concentration, J. Mol. Biol. 339, 185-197.
    • (2004) J. Mol. Biol. , vol.339 , pp. 185-197
    • Wandschneider, E.1    Bowler, B.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.