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Volumn 53, Issue 2, 2013, Pages 423-434

Do homologous thermophilic-mesophilic proteins exhibit similar structures and dynamics at optimal growth temperatures? a molecular dynamics simulation study

Author keywords

[No Author keywords available]

Indexed keywords

GROWTH TEMPERATURE; MOLECULAR DYNAMICS;

EID: 84874409618     PISSN: 15499596     EISSN: 1549960X     Source Type: Journal    
DOI: 10.1021/ci300474h     Document Type: Article
Times cited : (18)

References (72)
  • 1
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • Vieille, C.; Zeikus, G. J. 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.J.2
  • 2
    • 34047100353 scopus 로고    scopus 로고
    • Proteins from extremophiles as stable tools for advanced biotechnological applications of high social interest
    • de Champdoré, M.; Staiano, M.; Rossi, M.; D'Auria, S. Proteins from extremophiles as stable tools for advanced biotechnological applications of high social interest J. R. Soc. Interface 2007, 4, 183-191
    • (2007) J. R. Soc. Interface , vol.4 , pp. 183-191
    • De Champdoré, M.1    Staiano, M.2    Rossi, M.3    D'Auria, S.4
  • 3
    • 0029644328 scopus 로고
    • Hyperthermophiles: Taking the heat and loving it
    • Rees, D. C.; Adams, M. W. W. Hyperthermophiles: Taking the heat and loving it Structure 1995, 3, 251-254
    • (1995) Structure , vol.3 , pp. 251-254
    • Rees, D.C.1    Adams, M.W.W.2
  • 4
    • 0037424370 scopus 로고    scopus 로고
    • Activity-stability relationships in extremophilic enzymes
    • D'Amico, S.; Marx, J. C.; Gerday, C.; Feller, G. Activity-stability relationships in extremophilic enzymes J. Biol. Chem. 2003, 278, 7891-7896
    • (2003) J. Biol. Chem. , vol.278 , pp. 7891-7896
    • D'Amico, S.1    Marx, J.C.2    Gerday, C.3    Feller, G.4
  • 5
    • 0030741375 scopus 로고    scopus 로고
    • The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9 Å resolution
    • Russell, R. J. M.; Ferguson, J. M. C.; Hough, D. W.; Danson, M, J.; Taylor, G. L. The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9 Å resolution Biochemistry 1997, 36, 9983-9994
    • (1997) Biochemistry , vol.36 , pp. 9983-9994
    • Russell, R.J.M.1    Ferguson, J.M.C.2    Hough, D.W.3    Danson, M.J.4    Taylor, G.L.5
  • 6
    • 0038690122 scopus 로고    scopus 로고
    • Structures of thermophilic and mesophilic adenylate kinases from the genus Methanococcus
    • Criswell, A. R.; Bae, E.; Stec, B.; Konisky, J.; Phillips, G. N., Jr. Structures of thermophilic and mesophilic adenylate kinases from the genus Methanococcus J. Mol. Biol. 2003, 330, 1087-1099
    • (2003) J. Mol. Biol. , vol.330 , pp. 1087-1099
    • Criswell, A.R.1    Bae, E.2    Stec, B.3    Konisky, J.4    Phillips Jr., G.N.5
  • 7
    • 0017108645 scopus 로고
    • Deoxyribonucleic acid polymerase from the extreme thermophile Thermus aquaticus
    • Chien, A.; Edgar, D. B.; Trela, J. M. Deoxyribonucleic acid polymerase from the extreme thermophile Thermus aquaticus J. Bacteriol. 1976, 127, 1550-1557
    • (1976) J. Bacteriol. , vol.127 , pp. 1550-1557
    • Chien, A.1    Edgar, D.B.2    Trela, J.M.3
  • 8
    • 0035104931 scopus 로고    scopus 로고
    • Thermozymes and their applications: A review of recent literature and patents
    • Bruins, M. E.; Janssen, A. E.; Boom, R. M. Thermozymes and their applications: A review of recent literature and patents Appl. Biochem. Biotechnol. 2001, 90, 155-186
    • (2001) Appl. Biochem. Biotechnol. , vol.90 , pp. 155-186
    • Bruins, M.E.1    Janssen, A.E.2    Boom, R.M.3
  • 9
    • 34147150667 scopus 로고    scopus 로고
    • Potential and utilization of thermophiles and thermostable enzymes in biorefining
    • Turner, P.; Mamo, G.; Karlsson, E. N. Potential and utilization of thermophiles and thermostable enzymes in biorefining Microb. Cell. Fact. 2007, 6, 9-31
    • (2007) Microb. Cell. Fact. , vol.6 , pp. 9-31
    • Turner, P.1    Mamo, G.2    Karlsson, E.N.3
  • 11
    • 0041387567 scopus 로고    scopus 로고
    • A Large Scale Test of Computational Protein Design: Folding and Stability of Nine Completely Redesigned Globular Proteins
    • Dantas, G.; Kuhlman, B.; Callender, D.; Wong, M.; Baker, D. A Large Scale Test of Computational Protein Design: Folding and Stability of Nine Completely Redesigned Globular Proteins J. Mol. Biol. 2003, 332, 449-460
    • (2003) J. Mol. Biol. , vol.332 , pp. 449-460
    • Dantas, G.1    Kuhlman, B.2    Callender, D.3    Wong, M.4    Baker, D.5
  • 13
    • 18244373419 scopus 로고    scopus 로고
    • Computational thermostabilization of an enzyme
    • Korkegian, A.; Black, M. E.; Baker, D.; Stoddard, B. L. Computational thermostabilization of an enzyme Science 2005, 308, 857-860
    • (2005) Science , vol.308 , pp. 857-860
    • Korkegian, A.1    Black, M.E.2    Baker, D.3    Stoddard, B.L.4
  • 14
    • 33746546176 scopus 로고    scopus 로고
    • Simple electrostatic model improves designed protein sequences
    • Zollars, E. S.; Marshall, S. A.; Mayo, S. L. Simple electrostatic model improves designed protein sequences Protein Sci. 2006, 15, 2014-2018
    • (2006) Protein Sci. , vol.15 , pp. 2014-2018
    • Zollars, E.S.1    Marshall, S.A.2    Mayo, S.L.3
  • 15
    • 46249096540 scopus 로고    scopus 로고
    • Predicting protein thermostability changes from sequence upon multiple mutations
    • Montanucci, L.; Fariselli, P.; Martelli, P. L.; Casadio, R. Predicting protein thermostability changes from sequence upon multiple mutations Bioinformatics 2008, 24, i190-i195
    • (2008) Bioinformatics , vol.24
    • Montanucci, L.1    Fariselli, P.2    Martelli, P.L.3    Casadio, R.4
  • 17
    • 68149168637 scopus 로고    scopus 로고
    • Turning a mesophilic Protein into a Thermophilic one: A Computational Approach based on 3D structural features
    • Basu, S.; Sen, S. Turning a mesophilic Protein into a Thermophilic one: A Computational Approach based on 3D structural features J. Chem. Inf. Model. 2009, 49, 1741-1750
    • (2009) J. Chem. Inf. Model. , vol.49 , pp. 1741-1750
    • Basu, S.1    Sen, S.2
  • 18
    • 85050907599 scopus 로고    scopus 로고
    • Designing thermophilic proteins: A structure-based computational approach.
    • Sen, S. Nilsson, L. Francis & Taylor: CRC Press, USA, Chapter-6
    • Basu, S.; Sen, S. Designing thermophilic proteins: A structure-based computational approach. In Thermostable Proteins: Structural Stability and Design; Sen, S.; Nilsson, L., Eds.; Francis & Taylor: CRC Press, USA, 2011; Chapter-6, pp 117-153.
    • (2011) Thermostable Proteins: Structural Stability and Design , pp. 117-153
    • Basu, S.1    Sen, S.2
  • 19
    • 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
  • 20
    • 0031731672 scopus 로고    scopus 로고
    • Proteins from thermophilic and mesophilic organisms essentially do not differ in packing
    • Karshikoff, A.; Ladenstein, R. Proteins from thermophilic and mesophilic organisms essentially do not differ in packing Protein Eng. 1998, 11, 867-872
    • (1998) Protein Eng. , vol.11 , pp. 867-872
    • Karshikoff, A.1    Ladenstein, R.2
  • 22
    • 0034724271 scopus 로고    scopus 로고
    • Do ultrastable proteins from hyperthermophiles have high or low conformational rigidity?
    • Jaenicke, R. Do ultrastable proteins from hyperthermophiles have high or low conformational rigidity? Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 2926-2964
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 2926-2964
    • Jaenicke, R.1
  • 23
    • 0039116206 scopus 로고    scopus 로고
    • Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: Results of a comparative survey
    • Szilagyi, A.; Zavodszky, P. Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comparative survey Structure 2000, 8, 493-504
    • (2000) Structure , vol.8 , pp. 493-504
    • Szilagyi, A.1    Zavodszky, P.2
  • 24
    • 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
  • 25
    • 0035914477 scopus 로고    scopus 로고
    • Electrostatic stabilization of a thermophilic cold shock protein
    • Perl, D.; Schmid, F. X. Electrostatic stabilization of a thermophilic cold shock protein J. Mol. Biol. 2001, 313, 343-357
    • (2001) J. Mol. Biol. , vol.313 , pp. 343-357
    • Perl, D.1    Schmid, F.X.2
  • 26
    • 4444362321 scopus 로고    scopus 로고
    • An electrostatic basis for the stability of thermophilic proteins
    • Dominy, B. N.; Minoux, H.; Brooks, C. L., 3rd An electrostatic basis for the stability of thermophilic proteins Proteins 2004, 5, 128-141
    • (2004) Proteins , vol.5 , pp. 128-141
    • Dominy, B.N.1    Minoux, H.2    Brooks Iii, C.L.3
  • 27
    • 1242319481 scopus 로고    scopus 로고
    • Molecular simulations suggest protein salt bridges are uniquely suited to life at high temperatures
    • Thomas, A. S.; Elcock, A. H. Molecular simulations suggest protein salt bridges are uniquely suited to life at high temperatures J. Am. Chem. Soc. 2004, 126, 2208-2214
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 2208-2214
    • Thomas, A.S.1    Elcock, A.H.2
  • 28
    • 33745726737 scopus 로고    scopus 로고
    • Lessons in stability from thermophilic proteins
    • Razvi, A.; Scholtz, J. M. Lessons in stability from thermophilic proteins Protein Sci. 2006, 15, 1569-1578
    • (2006) Protein Sci. , vol.15 , pp. 1569-1578
    • Razvi, A.1    Scholtz, J.M.2
  • 29
    • 33846586937 scopus 로고    scopus 로고
    • Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins
    • Gribenko, A. V; Makhatadze, G. I. Role of the charge-charge interactions in defining stability and halophilicity of the CspB proteins J. Mol. Biol. 2007, 366, 842-856
    • (2007) J. Mol. Biol. , vol.366 , pp. 842-856
    • Gribenko, A.V.1    Makhatadze, G.I.2
  • 30
    • 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
  • 31
    • 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
  • 32
    • 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
  • 33
    • 32044454841 scopus 로고    scopus 로고
    • Effective factors in thermostability of thermophilic proteins
    • Sadeghi, M.; Naderi-Manesh, H.; Zarrabi, M.; Ranjbar, B. Effective factors in thermostability of thermophilic proteins Biophys. Chem. 2006, 119, 256-270
    • (2006) Biophys. Chem. , vol.119 , pp. 256-270
    • Sadeghi, M.1    Naderi-Manesh, H.2    Zarrabi, M.3    Ranjbar, B.4
  • 34
    • 34247193011 scopus 로고    scopus 로고
    • Mechanisms for stabilisation and the maintenance of solubility in proteins from thermophiles
    • Greaves, R. B.; Warwicker, J. Mechanisms for stabilisation and the maintenance of solubility in proteins from thermophiles BMC Struct. Biol. 2007, 7, 18-40
    • (2007) BMC Struct. Biol. , vol.7 , pp. 18-40
    • Greaves, R.B.1    Warwicker, J.2
  • 35
    • 0033994586 scopus 로고    scopus 로고
    • Electrostatic strengths of salt bridges in thermophilic and mesophilic glutamate dehydrogenase monomers
    • Kumar, S.; Ma, B.; Tsai, C. J.; Nussinov, R. Electrostatic strengths of salt bridges in thermophilic and mesophilic glutamate dehydrogenase monomers Proteins 2000, 38, 368-383
    • (2000) Proteins , vol.38 , pp. 368-383
    • Kumar, S.1    Ma, B.2    Tsai, C.J.3    Nussinov, R.4
  • 36
    • 0037432563 scopus 로고    scopus 로고
    • Contribution of surface salt bridges to protein stability: Guidelines for protein engineering
    • Makhatadze, G. I.; Loladze, V. V.; Ermolenko, D. N; Chen, X. F.; Thomas, S. T. Contribution of surface salt bridges to protein stability: Guidelines for protein engineering J. Mol. Biol. 2003, 327, 1135-1148
    • (2003) J. Mol. Biol. , vol.327 , pp. 1135-1148
    • Makhatadze, G.I.1    Loladze, V.V.2    Ermolenko, D.N.3    Chen, X.F.4    Thomas, S.T.5
  • 37
    • 0037083630 scopus 로고    scopus 로고
    • Molecular dynamics study of a hyperthermophilic and a mesophilic rubredoxin
    • Grottesi, A.; Ceruso, M. A.; Colosimo, A.; Di Nola, A. Molecular dynamics study of a hyperthermophilic and a mesophilic rubredoxin Proteins 2002, 46, 287-294
    • (2002) Proteins , vol.46 , pp. 287-294
    • Grottesi, A.1    Ceruso, M.A.2    Colosimo, A.3    Di Nola, A.4
  • 38
    • 24744447220 scopus 로고    scopus 로고
    • Identifying and Engineering Ion Pairs in Adenylate Kinases Insights from molecular dynamics simulations of thermophilic and mesophilic homologues
    • Bae, E.; Phillips, G. N., Jr. Identifying and Engineering Ion Pairs in Adenylate Kinases Insights from molecular dynamics simulations of thermophilic and mesophilic homologues J. Biol. Chem. 2005, 280, 30943-30948
    • (2005) J. Biol. Chem. , vol.280 , pp. 30943-30948
    • Bae, E.1    Phillips Jr., G.N.2
  • 39
    • 33744925655 scopus 로고    scopus 로고
    • Explanation of the Stability of Thermophilic Proteins Based on Unique Micromorphology
    • Melchionna, S.; Raffaele Sinibaldi, R.; Briganti, G. Explanation of the Stability of Thermophilic Proteins Based on Unique Micromorphology Biophys. J. 2006, 90, 4204-4212
    • (2006) Biophys. J. , vol.90 , pp. 4204-4212
    • Melchionna, S.1    Raffaele Sinibaldi, R.2    Briganti, G.3
  • 41
    • 77951143923 scopus 로고    scopus 로고
    • Temperature dependence of the flexibility of thermophilic and mesophilic flavoenzymes of the nitroreductase fold
    • Merkley, E. D.; William, W.; Parson, W. W.; Daggett, V. Temperature dependence of the flexibility of thermophilic and mesophilic flavoenzymes of the nitroreductase fold Prot. Eng., Des. Selec. 2010, 23, 327-336
    • (2010) Prot. Eng., Des. Selec. , vol.23 , pp. 327-336
    • Merkley, E.D.1    William, W.2    Parson, W.W.3    Daggett, V.4
  • 42
    • 79952455148 scopus 로고    scopus 로고
    • Dynamic properties of extremophilic subtilisin-like serine-proteases
    • Tiberti, M.; Papaleo, E. Dynamic properties of extremophilic subtilisin-like serine-proteases J. Struct. Biol. 2011, 174, 69-82
    • (2011) J. Struct. Biol. , vol.174 , pp. 69-82
    • Tiberti, M.1    Papaleo, E.2
  • 43
    • 84858320073 scopus 로고    scopus 로고
    • Dynamic Fingerprints of Protein Thermostability Revealed by Long Molecular Dynamics
    • Marcos, E.; Jimenez, A.; Crehuet, R. Dynamic Fingerprints of Protein Thermostability Revealed by Long Molecular Dynamics J. Chem. Theory Comput. 2012, 8, 1129-1142
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 1129-1142
    • Marcos, E.1    Jimenez, A.2    Crehuet, R.3
  • 44
    • 84858056832 scopus 로고    scopus 로고
    • Molecular Dynamics Simulations of a Hyperthermophilic and a Mesophilic Protein L30e
    • Lee, K. J. Molecular Dynamics Simulations of a Hyperthermophilic and a Mesophilic Protein L30e J. Chem. Inf. Model. 2012, 52, 7-15
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 7-15
    • Lee, K.J.1
  • 45
    • 84856833536 scopus 로고    scopus 로고
    • Thermophilic proteins: Insight and perspective from in silico experiments
    • Sterpone, F.; Melchionna, S. Thermophilic proteins: insight and perspective from in silico experiments Chem. Soc. Rev. 2012, 41, 1665-1676
    • (2012) Chem. Soc. Rev. , vol.41 , pp. 1665-1676
    • Sterpone, F.1    Melchionna, S.2
  • 46
    • 77951143923 scopus 로고    scopus 로고
    • Temperature dependence of the flexibility of thermophilic and mesophilic flavoenzymes of the nitroreductase fold
    • Merkley, E. D.; W.Parson, W. W.; Valerie Daggett, V. Temperature dependence of the flexibility of thermophilic and mesophilic flavoenzymes of the nitroreductase fold Prot. Eng. Des. Selec. 2010, 23, 327-336
    • (2010) Prot. Eng. Des. Selec. , vol.23 , pp. 327-336
    • Merkley, E.D.1    Parson, W.W.2    Valerie Daggett, V.3
  • 47
    • 77956912541 scopus 로고    scopus 로고
    • Protein stability and enzyme activity at extreme biological temperatures
    • Feller, G. Protein stability and enzyme activity at extreme biological temperatures J. Phys.: Condens. Matter 2010, 22, 323101
    • (2010) J. Phys.: Condens. Matter , vol.22 , pp. 323101
    • Feller, G.1
  • 48
    • 0027296211 scopus 로고
    • Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein
    • Schindelin, H.; Marahiel, M. A.; Heinemann, U. Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein Nature 1993, 364, 164-168
    • (1993) Nature , vol.364 , pp. 164-168
    • Schindelin, H.1    Marahiel, M.A.2    Heinemann, U.3
  • 49
    • 0034615784 scopus 로고    scopus 로고
    • Thermal stability and atomic-resolution crystal structure of the Bacillus caldolyticus cold shock protein
    • Müller, U.; Perl, D.; Schmid, F. X; Heinemann, U. Thermal stability and atomic-resolution crystal structure of the Bacillus caldolyticus cold shock protein J. Mol. Biol. 2000, 297, 975-988
    • (2000) J. Mol. Biol. , vol.297 , pp. 975-988
    • Müller, U.1    Perl, D.2    Schmid, F.X.3    Heinemann, U.4
  • 50
    • 0019500409 scopus 로고
    • Growth of bacteria at 100 C and beyond
    • Heinen, W.; Lauwers, A. M. Growth of bacteria at 100 C and beyond Arch. Microbiol. 1981, 129, 127-128
    • (1981) Arch. Microbiol. , vol.129 , pp. 127-128
    • Heinen, W.1    Lauwers, A.M.2
  • 51
    • 0035960641 scopus 로고    scopus 로고
    • Thermodynamic Differences among Homologous Thermophilic and Mesophilic Proteins
    • Kumar, S.; Tsai, C. J.; Nussinov, R. Thermodynamic Differences among Homologous Thermophilic and Mesophilic Proteins Biochemistry 2001, 40, 14152-14165
    • (2001) Biochemistry , vol.40 , pp. 14152-14165
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 53
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J. P.; Ciccotti, G.; Berendsen, H. J. C. Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes J. Comput. Phys. 1977, 23, 327-341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 54
    • 36449007976 scopus 로고
    • The effect of longrange electrostatic interactions in simulations of macromolecular crystals: A comparison of the Ewald and truncated list methods
    • York, D. M.; Darden, T. A.; Pedersen, L. G. The effect of longrange electrostatic interactions in simulations of macromolecular crystals: A comparison of the Ewald and truncated list methods J. Chem. Phys. 1993, 99, 8345-8348
    • (1993) J. Chem. Phys. , vol.99 , pp. 8345-8348
    • York, D.M.1    Darden, T.A.2    Pedersen, L.G.3
  • 55
    • 84986534166 scopus 로고
    • New spherical-cutoff methods for long-range forces in macromolecular simulation
    • Steinbach, P. J.; Brooks, B. R. New spherical-cutoff methods for long-range forces in macromolecular simulation J. Comput. Chem. 1994, 15, 667-683
    • (1994) J. Comput. Chem. , vol.15 , pp. 667-683
    • Steinbach, P.J.1    Brooks, B.R.2
  • 56
    • 0033850287 scopus 로고    scopus 로고
    • On the Truncation of Long-Range Electrostatic Interactions in DNA
    • Norberg, Y.; Nilsson, L. On the Truncation of Long-Range Electrostatic Interactions in DNA Biophys. J. 2000, 79, 1537-1553
    • (2000) Biophys. J. , vol.79 , pp. 1537-1553
    • Norberg, Y.1    Nilsson, L.2
  • 57
    • 0033654654 scopus 로고    scopus 로고
    • Molecular dynamics simulation of nucleic acids
    • Cheatham, T. E.; Kollman, P. E. Molecular dynamics simulation of nucleic acids Annu. Rev. Phys. Chem. 2000, 51, 435-471
    • (2000) Annu. Rev. Phys. Chem. , vol.51 , pp. 435-471
    • Cheatham, T.E.1    Kollman, P.E.2
  • 60
    • 0033613906 scopus 로고    scopus 로고
    • Native Proteins are Surface-molten Solids: Application of the Lindemann Criterion for the Solid versus Liquid State
    • Zhou, Y.; Vitkup, D.; Karplus, M. Native Proteins are Surface-molten Solids: Application of the Lindemann Criterion for the Solid versus Liquid State J. Mol. Biol. 1999, 285, 1371-1375
    • (1999) J. Mol. Biol. , vol.285 , pp. 1371-1375
    • Zhou, Y.1    Vitkup, D.2    Karplus, M.3
  • 61
    • 41849083678 scopus 로고
    • Dynamics at solid liquid transition - Experiments at the freezing-point
    • Bilgram, J. H. Dynamics at solid liquid transition-experiments at the freezing-point Phys. Rep. 1987, 153, 1-89
    • (1987) Phys. Rep. , vol.153 , pp. 1-89
    • Bilgram, J.H.1
  • 62
    • 0038679626 scopus 로고
    • Melting, freezing and colloidal suspensions
    • LoEwen, H. Melting, freezing and colloidal suspensions Phys. Rep. 1994, 237, 249-324
    • (1994) Phys. Rep. , vol.237 , pp. 249-324
    • Loewen, H.1
  • 63
    • 11344259128 scopus 로고
    • A topographic view of supercooled liquids and glass formation
    • Stillinger, F. H. A topographic view of supercooled liquids and glass formation Science 1995, 267, 1935-1939
    • (1995) Science , vol.267 , pp. 1935-1939
    • Stillinger, F.H.1
  • 64
    • 0001587354 scopus 로고
    • Computational study of transition dynamics in 55-atom clusters
    • Stillinger, F. H.; Stillinger, D. K. Computational study of transition dynamics in 55-atom clusters J. Chem. Phys. 1990, 93, 6013-6024
    • (1990) J. Chem. Phys. , vol.93 , pp. 6013-6024
    • Stillinger, F.H.1    Stillinger, D.K.2
  • 65
    • 0015222647 scopus 로고
    • The interpretation of protein structures. Estimation of static accessibility
    • Lee, B. K.; Richards, F. M. The interpretation of protein structures. Estimation of static accessibility J. Mol. Biol. 1971, 55, 379-400
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.K.1    Richards, F.M.2
  • 66
    • 0034100848 scopus 로고    scopus 로고
    • Two exposed amino acid residues confer thermostability on a cold shock protein
    • Perl, D.; Mueller, U.; Heinemann, U.; Schmid, F. X. Two exposed amino acid residues confer thermostability on a cold shock protein Nat. Struct. Biol. 2000, 7, 380-383
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 380-383
    • Perl, D.1    Mueller, U.2    Heinemann, U.3    Schmid, F.X.4
  • 67
    • 0000020246 scopus 로고    scopus 로고
    • A five-site model for liquid water and the reproduction of the density anomaly by rigid, non-polarizable potential functions
    • Mahoney, M. W.; Jorgensen, W. L. A five-site model for liquid water and the reproduction of the density anomaly by rigid, non-polarizable potential functions J. Chem. Phys. 2000, 112, 8910-8920
    • (2000) J. Chem. Phys. , vol.112 , pp. 8910-8920
    • Mahoney, M.W.1    Jorgensen, W.L.2
  • 68
    • 0034662899 scopus 로고    scopus 로고
    • The radial distribution functions of water and ice from 220 to 673 K and at pressures up to 400 MPa
    • Soper, A. K. The radial distribution functions of water and ice from 220 to 673 K and at pressures up to 400 MPa Chem. Phys. 2000, 258, 121-137
    • (2000) Chem. Phys. , vol.258 , pp. 121-137
    • Soper, A.K.1
  • 69
    • 0024970964 scopus 로고
    • Catalytic properties of thermophilic lactate dehydrogenase and halophilic malate dehydrogenase at high temperature and low water activity
    • Hecht, K.; Wrba, A.; Jaenicke, R. Catalytic properties of thermophilic lactate dehydrogenase and halophilic malate dehydrogenase at high temperature and low water activity Eur. J. Biochem. 1989, 183, 69-74
    • (1989) Eur. J. Biochem. , vol.183 , pp. 69-74
    • Hecht, K.1    Wrba, A.2    Jaenicke, R.3
  • 70
    • 2542487312 scopus 로고    scopus 로고
    • Multiple time scale backbone dynamics of homologous thermophilic and mesophilic ribonuclease HI enzymes
    • Butterwick, J. A.; Loria, J. P.; Astrof, N. S.; Kroenke, C. D.; Cole, R.; Rance, M.; Palmer, A. G., III. Multiple time scale backbone dynamics of homologous thermophilic and mesophilic ribonuclease HI enzymes J. Mol. Biol. 2004, 339, 855-871
    • (2004) J. Mol. Biol. , vol.339 , pp. 855-871
    • Butterwick, J.A.1    Loria, J.P.2    Astrof, N.S.3    Kroenke, C.D.4    Cole, R.5    Rance, M.6    Palmer Iii, A.G.7
  • 71
    • 45849083521 scopus 로고    scopus 로고
    • Protein Dynamics and Stability: The Distribution of Atomic Fluctuations in Thermophilic and Mesophilic Dihydrofolate Reductase Derived Using Elastic Incoherent Neutron Scattering
    • Meinhold, L.; Clement, D.; Tehei, M.; Daniel, R.; Finney, J. L.; Smith, J. C. Protein Dynamics and Stability: The Distribution of Atomic Fluctuations in Thermophilic and Mesophilic Dihydrofolate Reductase Derived Using Elastic Incoherent Neutron Scattering Biophys. J. 2008, 94, 4812-4818
    • (2008) Biophys. J. , vol.94 , pp. 4812-4818
    • Meinhold, L.1    Clement, D.2    Tehei, M.3    Daniel, R.4    Finney, J.L.5    Smith, J.C.6


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