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Volumn 48, Issue 1, 2008, Pages 119-127

Thermostability of salt bridges versus hydrophobic interactions in proteins probed by statistical potentials

Author keywords

[No Author keywords available]

Indexed keywords

HYDROPHOBICITY; PROTEINS; STATISTICAL METHODS; THERMODYNAMIC STABILITY;

EID: 39449128325     PISSN: 15499596     EISSN: 1549960X     Source Type: Journal    
DOI: 10.1021/ci700237g     Document Type: Article
Times cited : (59)

References (42)
  • 3
    • 0037411739 scopus 로고    scopus 로고
    • Developments in industrially important thermostable enzymes: A review
    • Haki, G. D.; Rakshit, S. K. Developments in industrially important thermostable enzymes: a review. Bioresour. Technol. 2003, 89, 17-34.
    • (2003) Bioresour. Technol , vol.89 , pp. 17-34
    • Haki, G.D.1    Rakshit, S.K.2
  • 5
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, and ion pairs
    • Vogt, G.; Woell, S.; Argos, P. Protein thermal stability, hydrogen bonds, and ion pairs. J. Mol. Biol. 1997, 269, 631-643.
    • (1997) J. Mol. Biol , vol.269 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 6
    • 0033214040 scopus 로고    scopus 로고
    • Analysis of thermal stabilizing interactions in mesophilic and thermophilic adenylate kinases from the genus Methanococcus
    • Haney, P. J.; Stees, M.; Konisky, J. Analysis of thermal stabilizing interactions in mesophilic and thermophilic adenylate kinases from the genus Methanococcus. J. Biol. Chem. 1999, 274, 28453-28458.
    • (1999) J. Biol. Chem , vol.274 , pp. 28453-28458
    • Haney, P.J.1    Stees, M.2    Konisky, J.3
  • 7
    • 0034693042 scopus 로고    scopus 로고
    • Structural and genomic correlates of hyperthermostability
    • Cambillau, C.; Claverie, J.-M. Structural and genomic correlates of hyperthermostability. J. Biol. Chem. 2000, 275, 32383-32386.
    • (2000) J. Biol. Chem , vol.275 , pp. 32383-32386
    • Cambillau, C.1    Claverie, J.-M.2
  • 8
    • 0034495733 scopus 로고    scopus 로고
    • Aromatic clusters: A determinant of thermal stability of thermophilic proteins
    • Kannan, N.; Vishveshwara, S. Aromatic clusters: a determinant of thermal stability of thermophilic proteins. Protein Eng. 2000, 13, 753-761.
    • (2000) Protein Eng , vol.13 , pp. 753-761
    • Kannan, N.1    Vishveshwara, S.2
  • 9
    • 0034017055 scopus 로고    scopus 로고
    • Factors enhancing protein thermostability
    • Kumar, S.; Tsai, C.-J.; Nussinov, R. Factors enhancing protein thermostability. Protein Eng. 2000, 13, 179-191.
    • (2000) Protein Eng , vol.13 , pp. 179-191
    • Kumar, S.1    Tsai, C.-J.2    Nussinov, R.3
  • 10
    • 0039116206 scopus 로고    scopus 로고
    • Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: Results of a comprehensive survey
    • Szilágyi, A.; Závodszky, P. Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey. Structure 2000, 8, 493-504.
    • (2000) Structure , vol.8 , pp. 493-504
    • Szilágyi, A.1    Závodszky, P.2
  • 11
    • 0034997442 scopus 로고    scopus 로고
    • Structural adaptation of enzymes to low temperatures
    • Gianese, G.; Argos, P.; Pascarella, S. Structural adaptation of enzymes to low temperatures. Protein Eng. 2001, 14, 141-148.
    • (2001) Protein Eng , vol.14 , pp. 141-148
    • Gianese, G.1    Argos, P.2    Pascarella, S.3
  • 12
    • 0037172796 scopus 로고    scopus 로고
    • Elucidation of factors responsible for enhanced thermal stability of proteins: A structural genomics based study
    • Chakravarty, S.; Varadarajan, R. Elucidation of factors responsible for enhanced thermal stability of proteins: A structural genomics based study. Biochemistry 2002, 41, 8152-8161.
    • (2002) Biochemistry , vol.41 , pp. 8152-8161
    • Chakravarty, S.1    Varadarajan, R.2
  • 13
    • 0036568335 scopus 로고    scopus 로고
    • Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes
    • Gianese, G.; Bossa, F.; Pascarella, S. Comparative structural analysis of psychrophilic and meso- and thermophilic enzymes. Proteins 2002, 47, 236-249.
    • (2002) Proteins , vol.47 , pp. 236-249
    • Gianese, G.1    Bossa, F.2    Pascarella, S.3
  • 14
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • Vieille, C.; Zeikus, G. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol. Mol. Biol. Rev. 2001, 65, 1-43.
    • (2001) Microbiol. Mol. Biol. Rev , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.2
  • 15
    • 0016771835 scopus 로고
    • Stereochemical basis of heat stability in bacterial ferrodoxins and in haemoglobin A2
    • Perutz, M. F.; Raidt, H. Stereochemical basis of heat stability in bacterial ferrodoxins and in haemoglobin A2. Nature 1975, 255, 256-259.
    • (1975) Nature , vol.255 , pp. 256-259
    • Perutz, M.F.1    Raidt, H.2
  • 16
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? A continuum electrostatic analysis
    • Hendsch, Z. S.; Tidor, B. Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Sci. 1994, 3, 211-226.
    • (1994) Protein Sci , vol.3 , pp. 211-226
    • Hendsch, Z.S.1    Tidor, B.2
  • 17
    • 0032573431 scopus 로고    scopus 로고
    • The stability of salt bridges at high temperatures: Implications of hyperthermophilic proteins
    • Elcock, A. H. The stability of salt bridges at high temperatures: implications of hyperthermophilic proteins. J. Mol. Biol. 1998, 284, 489-502.
    • (1998) J. Mol. Biol , vol.284 , pp. 489-502
    • Elcock, A.H.1
  • 18
    • 0036902235 scopus 로고    scopus 로고
    • Close-range electrostatic interactions in proteins
    • Kumar, S.; Nussinov, R. Close-range electrostatic interactions in proteins. ChemBioChem 2002, 3, 604-617.
    • (2002) ChemBioChem , vol.3 , pp. 604-617
    • Kumar, S.1    Nussinov, R.2
  • 19
    • 0033550299 scopus 로고    scopus 로고
    • Salt bridge stability in monomelic proteins
    • Kumar, S.; Nussinov, R. Salt bridge stability in monomelic proteins. J. Mol. Biol. 1999, 293, 1241-1255.
    • (1999) J. Mol. Biol , vol.293 , pp. 1241-1255
    • Kumar, S.1    Nussinov, R.2
  • 21
    • 0029588555 scopus 로고
    • Complex salt bridges in proteins: Statistical analysis of structure and function
    • Musafia, B.; Buchner, V.; Arad, D. Complex salt bridges in proteins: statistical analysis of structure and function. J. Mol. Biol. 1995, 254, 761-770.
    • (1995) J. Mol. Biol , vol.254 , pp. 761-770
    • Musafia, B.1    Buchner, V.2    Arad, D.3
  • 22
    • 0033603392 scopus 로고    scopus 로고
    • Electrostatic contributions to the stability of hypertheromphilic proteins
    • Xiao, L.; Honig, B. Electrostatic contributions to the stability of hypertheromphilic proteins. J. Mol. Biol. 1999, 289, 1435-1444.
    • (1999) J. Mol. Biol , vol.289 , pp. 1435-1444
    • Xiao, L.1    Honig, B.2
  • 23
    • 0347927627 scopus 로고    scopus 로고
    • Preliminary characterization and crystal structure of a thermostable cytochrome P450 from Thermus thermophilus
    • Yano, J. K.; Blasco, F.; Li, H.; Schmid, R. D.; Henne, A.; Poulos, T. L. Preliminary characterization and crystal structure of a thermostable cytochrome P450 from Thermus thermophilus. J. Biol. Chem. 2003, 278, 608-616.
    • (2003) J. Biol. Chem , vol.278 , pp. 608-616
    • Yano, J.K.1    Blasco, F.2    Li, H.3    Schmid, R.D.4    Henne, A.5    Poulos, T.L.6
  • 24
    • 0035876847 scopus 로고    scopus 로고
    • Important inter-residue contacts for enhancing the thermal stability of thermophilic proteins
    • Gromiha, M. M. Important inter-residue contacts for enhancing the thermal stability of thermophilic proteins. Biophys. Chem. 2001, 91, 71-77.
    • (2001) Biophys. Chem , vol.91 , pp. 71-77
    • Gromiha, M.M.1
  • 25
    • 0029932580 scopus 로고    scopus 로고
    • Analysis of protein characteristics related to thermostability
    • Querol, E.; Perez-Pons, J. A.; Mozo-Villarias, A. Analysis of protein characteristics related to thermostability. Protein Eng. 1996, 9, 265-271.
    • (1996) Protein Eng , vol.9 , pp. 265-271
    • Querol, E.1    Perez-Pons, J.A.2    Mozo-Villarias, A.3
  • 26
    • 0030970741 scopus 로고    scopus 로고
    • Structural basis for thermostability and identification of potential active residues for adenilate kinase from archaeal genus Methanococcus
    • Haney, P.; Konisky, J.; Koretke, K. K.; Luthey-Schulten, Z.; Wolynes, P. G. Structural basis for thermostability and identification of potential active residues for adenilate kinase from archaeal genus Methanococcus. Proteins 1997, 28, 117-130.
    • (1997) Proteins , vol.28 , pp. 117-130
    • Haney, P.1    Konisky, J.2    Koretke, K.K.3    Luthey-Schulten, Z.4    Wolynes, P.G.5
  • 28
    • 24644472817 scopus 로고    scopus 로고
    • Physics and evolution of thermophilic adaptation
    • Berezovsky, I., and Shakhnovich, E. I. Physics and evolution of thermophilic adaptation. Proc. Natl. Acad. Sci., USA 2005, 102, 12742-12747.
    • (2005) Proc. Natl. Acad. Sci., USA , vol.102 , pp. 12742-12747
    • Berezovsky, I.1    Shakhnovich, E.I.2
  • 29
    • 0346104820 scopus 로고    scopus 로고
    • The universal ancestor and the ancestor of bacteria were hyperthermophiles
    • Di Giulio, M. The universal ancestor and the ancestor of bacteria were hyperthermophiles. J. Mol. Evol. 2003, 57, 721-730.
    • (2003) J. Mol. Evol , vol.57 , pp. 721-730
    • Di Giulio, M.1
  • 30
    • 0032715527 scopus 로고    scopus 로고
    • Important amino acid properties for enhanced thermostability from mesophilic to thermophilic proteins
    • Gromiha, M. M.; Oobatake, M.; Sarai, A. Important amino acid properties for enhanced thermostability from mesophilic to thermophilic proteins. Biophys. Chem. 1999, 82, 51-67.
    • (1999) Biophys. Chem , vol.82 , pp. 51-67
    • Gromiha, M.M.1    Oobatake, M.2    Sarai, A.3
  • 32
    • 0032169688 scopus 로고    scopus 로고
    • Henrick, K.; Thornton, J. M. PQS: a protein quaternary structure file server. Trends Biochem. Sci. 1998, 23, 358-361.
    • Henrick, K.; Thornton, J. M. PQS: a protein quaternary structure file server. Trends Biochem. Sci. 1998, 23, 358-361.
  • 33
    • 0043180474 scopus 로고    scopus 로고
    • PISCES: A protein sequence culling server
    • Wang, G.; Dunbrack, R. L. PISCES: a protein sequence culling server. Bioinformatics 2003, 19, 1589-1591.
    • (2003) Bioinformatics , vol.19 , pp. 1589-1591
    • Wang, G.1    Dunbrack, R.L.2
  • 34
    • 0025341310 scopus 로고
    • Calculation of conformational ensembles from potentials of mean force. An approach to the knowledge-based prediction of local structures in globular proteins
    • Sippl, M. J. Calculation of conformational ensembles from potentials of mean force. An approach to the knowledge-based prediction of local structures in globular proteins. J. Mol. Biol. 1990, 213, 859-883.
    • (1990) J. Mol. Biol , vol.213 , pp. 859-883
    • Sippl, M.J.1
  • 35
    • 0028318094 scopus 로고
    • Factors influencing the ability of knowledge based potentials to identify native sequence-structure matches
    • Kocher, J.-P.; Rooman, M.; Wodak, S. Factors influencing the ability of knowledge based potentials to identify native sequence-structure matches. J. Mol. Biol. 1994, 235, 1598-1613.
    • (1994) J. Mol. Biol , vol.235 , pp. 1598-1613
    • Kocher, J.-P.1    Rooman, M.2    Wodak, S.3
  • 36
    • 33744906496 scopus 로고    scopus 로고
    • A new generation of statistical potentials for proteins
    • Dehouck, Y.; Gilis, D.; Rooman, M. A new generation of statistical potentials for proteins. Biophys. J. 2006, 90, 4010-4017.
    • (2006) Biophys. J , vol.90 , pp. 4010-4017
    • Dehouck, Y.1    Gilis, D.2    Rooman, M.3
  • 38
    • 0028304962 scopus 로고
    • Satisfying bonding potential in proteins
    • McDonald, I. K.; Thornton, J. M. Satisfying bonding potential in proteins. J. Mol. Biol.1994, 238, 777-793.
    • (1994) J. Mol. Biol , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 40
    • 0037816903 scopus 로고    scopus 로고
    • Computed-aided methods of evaluating thermodynamic and thermal stability changes of proteins
    • Gilis, D.; Wintjens, R.; Rooman, M. Computed-aided methods of evaluating thermodynamic and thermal stability changes of proteins. Res. Devel. Protein Eng. 2001, 1, 277-290.
    • (2001) Res. Devel. Protein Eng , vol.1 , pp. 277-290
    • Gilis, D.1    Wintjens, R.2    Rooman, M.3
  • 41
    • 3042733153 scopus 로고    scopus 로고
    • Database-derived potentials dependent on protein size for in silico folding and design
    • Dehouck, Y.; Gilis, D.; Rooman, M. Database-derived potentials dependent on protein size for in silico folding and design. Biophys. J. 2004, 87, 171-181.
    • (2004) Biophys. J , vol.87 , pp. 171-181
    • Dehouck, Y.1    Gilis, D.2    Rooman, M.3
  • 42
    • 39449129654 scopus 로고    scopus 로고
    • DeLano, W. L. The PyMOL Molecular Graphics System. DeLano Scientific, San Carlos, CA, 2002 (URL: http://www.pymol.org/).
    • DeLano, W. L. The PyMOL Molecular Graphics System. DeLano Scientific, San Carlos, CA, 2002 (URL: http://www.pymol.org/).


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