메뉴 건너뛰기




Volumn 53, Issue 9, 2013, Pages 2448-2461

Molecular dynamics perspective on the protein thermal stability: A case study using SAICAR synthetase

Author keywords

[No Author keywords available]

Indexed keywords

DIMERS; ENZYMES; HYDROGEN BONDS; HYDROPHOBICITY;

EID: 84884561782     PISSN: 15499596     EISSN: 1549960X     Source Type: Journal    
DOI: 10.1021/ci400306m     Document Type: Article
Times cited : (28)

References (65)
  • 1
    • 33750040585 scopus 로고    scopus 로고
    • Hyperthermophiles in the history of life
    • Stetter, K. O. Hyperthermophiles in the history of life Philos. Trans. R. Soc. London, Ser. B 2006, 361 (1474) 1837-1843
    • (2006) Philos. Trans. R. Soc. London, Ser. B , vol.361 , Issue.1474 , pp. 1837-1843
    • Stetter, K.O.1
  • 2
    • 81055147626 scopus 로고    scopus 로고
    • Molecular bases of thermophily in hyperthermophiles
    • Imanaka, T. Molecular bases of thermophily in hyperthermophiles Proc. Jpn. Acad., Ser. B 2011, 87 (9) 587-602
    • (2011) Proc. Jpn. Acad., Ser. B , vol.87 , Issue.9 , pp. 587-602
    • Imanaka, T.1
  • 3
    • 0016771835 scopus 로고
    • Stereochemical basis of heat stability in bacterial ferredoxins and in hemoglobin A2
    • Perutz, M. F.; Raidt, H. Stereochemical basis of heat stability in bacterial ferredoxins and in hemoglobin A2 Nature 1975, 255 (5505) 256-259
    • (1975) Nature , vol.255 , Issue.5505 , pp. 256-259
    • Perutz, M.F.1    Raidt, H.2
  • 4
    • 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) 1-43
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , Issue.1 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 5
    • 0026320363 scopus 로고
    • Nonenzymatic deamidation of asparaginyl and glutamyl residues in proteins
    • Wright, H. T. Nonenzymatic deamidation of asparaginyl and glutamyl residues in proteins Crit. Rev. Biochem. Mol. Biol. 1991, 26 (1) 1-52
    • (1991) Crit. Rev. Biochem. Mol. Biol. , vol.26 , Issue.1 , pp. 1-52
    • Wright, H.T.1
  • 6
    • 0023055754 scopus 로고
    • Why does ribonuclease irreversibly inactivate at high temperatures?
    • Zale, S. E.; Klibanov, A. M. Why does ribonuclease irreversibly inactivate at high temperatures? Biochemistry 1986, 25 (19) 5432-5444
    • (1986) Biochemistry , vol.25 , Issue.19 , pp. 5432-5444
    • Zale, S.E.1    Klibanov, A.M.2
  • 7
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • Jaenicke, R.; Böhm, G. The stability of proteins in extreme environments Curr. Opin. Struct. Biol. 1998, 8 (6) 738-748
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , Issue.6 , pp. 738-748
    • Jaenicke, R.1    Böhm, G.2
  • 8
    • 0033616712 scopus 로고    scopus 로고
    • Thermal adaptation analyzed by comparison of protein sequences from mesophilic and extremely thermophilic Methanococcus species
    • Haney, P. J.; Badger, J. H.; Buldak, G. L.; Reich, C. I.; Woese, C. R.; Olsen, G. J. Thermal adaptation analyzed by comparison of protein sequences from mesophilic and extremely thermophilic Methanococcus species Proc. Natl. Acad. Sci. U.S.A. 1999, 96 (7) 3578-3583
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , Issue.7 , pp. 3578-3583
    • Haney, P.J.1    Badger, J.H.2    Buldak, G.L.3    Reich, C.I.4    Woese, C.R.5    Olsen, G.J.6
  • 10
    • 0031686238 scopus 로고    scopus 로고
    • Helix stabilizing factors and stabilization of thermophilic proteins: An X-ray based study
    • Facchiano, A. M.; Colonna, G.; Ragone, R. Helix stabilizing factors and stabilization of thermophilic proteins: an X-ray based study Protein Eng. 1998, 11 (9) 753-760
    • (1998) Protein Eng. , vol.11 , Issue.9 , pp. 753-760
    • Facchiano, A.M.1    Colonna, G.2    Ragone, R.3
  • 11
    • 0033534477 scopus 로고    scopus 로고
    • Extremely thermostable serine-type protease from Aquifex pyrophilus. Molecular cloning, expression, and characterization
    • Choi, I.-G.; Bang, W.-G.; Kim, S.-H.; Yu, Y. G. Extremely thermostable serine-type protease from Aquifex pyrophilus. Molecular cloning, expression, and characterization J. Biol. Chem. 1999, 274 (2) 881-888
    • (1999) J. Biol. Chem. , vol.274 , Issue.2 , pp. 881-888
    • Choi, I.-G.1    Bang, W.-G.2    Kim, S.-H.3    Yu, Y.G.4
  • 12
    • 0033538553 scopus 로고    scopus 로고
    • Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostability
    • Thompson, M. J.; Eisenberg, D. Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostability J. Mol. Biol. 1999, 290 (2) 595-604
    • (1999) J. Mol. Biol. , vol.290 , Issue.2 , pp. 595-604
    • Thompson, M.J.1    Eisenberg, D.2
  • 13
  • 14
    • 0026777217 scopus 로고
    • Contribution of the hydrophobic effect to globular protein stability
    • Pace, C. N. Contribution of the hydrophobic effect to globular protein stability J. Mol. Biol. 1992, 226 (1) 29-35
    • (1992) J. Mol. Biol. , vol.226 , Issue.1 , pp. 29-35
    • Pace, C.N.1
  • 15
    • 34548383957 scopus 로고    scopus 로고
    • Amino-acid interactions in psychrophiles, mesophiles, thermophiles and hyperthermophiles: Insights from the quasi-chemical approximations
    • Goldstein, R. A. Amino-acid interactions in psychrophiles, mesophiles, thermophiles and hyperthermophiles: Insights from the quasi-chemical approximations Protein Sci. 2007, 16 (9) 1887-1895
    • (2007) Protein Sci. , vol.16 , Issue.9 , pp. 1887-1895
    • Goldstein, R.A.1
  • 16
    • 41149102801 scopus 로고    scopus 로고
    • Hydrophobic effect on the stability and folding of a hyperthermophilic protein
    • Dong, H.; Mukaiyama, A.; Tadokoro, T.; Koga, Y.; Takano, K.; Kanaya, S. Hydrophobic effect on the stability and folding of a hyperthermophilic protein J. Mol. Biol. 2008, 378 (1) 264-272
    • (2008) J. Mol. Biol. , vol.378 , Issue.1 , pp. 264-272
    • Dong, H.1    Mukaiyama, A.2    Tadokoro, T.3    Koga, Y.4    Takano, K.5    Kanaya, S.6
  • 17
    • 42149186292 scopus 로고    scopus 로고
    • "hot cores" in proteins: Comparative analysis of the polar contact area in structures from hyper/thermophilic and mesophilic organisms
    • Paiardini, A.; Sali, R.; Bossa, F.; Pascarella, S. "Hot cores" in proteins: comparative analysis of the polar contact area in structures from hyper/thermophilic and mesophilic organisms BMC Struct. Biol. 2008, 8, 14
    • (2008) BMC Struct. Biol. , vol.8 , pp. 14
    • Paiardini, A.1    Sali, R.2    Bossa, F.3    Pascarella, S.4
  • 18
    • 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 (11) 753-761
    • (2000) Protein Eng. , vol.13 , Issue.11 , pp. 753-761
    • Kannan, N.1    Vishveshwara, S.2
  • 19
    • 8444244797 scopus 로고    scopus 로고
    • Role of weak interactions in thermal stability of proteins
    • Ibrahim, B. S.; Pattabhi, V. Role of weak interactions in thermal stability of proteins Biochem. Biophys. Res. Commun. 2004, 325 (3) 1082-1089
    • (2004) Biochem. Biophys. Res. Commun. , vol.325 , Issue.3 , pp. 1082-1089
    • Ibrahim, B.S.1    Pattabhi, V.2
  • 21
    • 0033603392 scopus 로고    scopus 로고
    • Electrostatic contribution to the stability of hyperthermophilic proteins
    • Xiao, L.; Honig, B. Electrostatic contribution to the stability of hyperthermophilic proteins J. Mol. Biol. 1999, 289 (5) 1435-1444
    • (1999) J. Mol. Biol. , vol.289 , Issue.5 , pp. 1435-1444
    • Xiao, L.1    Honig, B.2
  • 22
    • 0034017055 scopus 로고    scopus 로고
    • Factors enhancing protein thermostability
    • Kumar, S.; Tsai, C.-J.; Nussinov, R. Factors enhancing protein thermostability Protein Eng. 2000, 13 (3) 179-191
    • (2000) Protein Eng. , vol.13 , Issue.3 , pp. 179-191
    • Kumar, S.1    Tsai, C.-J.2    Nussinov, R.3
  • 23
    • 0039116206 scopus 로고    scopus 로고
    • Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: Results of a comprehensive survey
    • Szilàgyi, A.; Závodszky, P. Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey Structure 2000, 8 (5) 493-504
    • (2000) Structure , vol.8 , Issue.5 , pp. 493-504
    • Szilàgyi, A.1    Závodszky, P.2
  • 24
    • 0035448574 scopus 로고    scopus 로고
    • Ion pairs and the thermotolerance of proteins from hyperthermophiles: "traffic rule" for hot roads
    • Karshikoff, A.; Ladenstein, R. Ion pairs and the thermotolerance of proteins from hyperthermophiles: "traffic rule" for hot roads Trends Biochem. Sci. 2001, 26 (9) 550-556
    • (2001) Trends Biochem. Sci. , vol.26 , Issue.9 , pp. 550-556
    • Karshikoff, A.1    Ladenstein, R.2
  • 25
    • 0011186093 scopus 로고    scopus 로고
    • Protein thermal stability: Hydrogen bonds or internal packing?
    • Vogt, G.; Argos, P. Protein thermal stability: hydrogen bonds or internal packing? Struct. Fold. Des. 1997, 2 (4) S40-S46
    • (1997) Struct. Fold. Des. , vol.2 , Issue.4
    • Vogt, G.1    Argos, P.2
  • 26
    • 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 (4) 631-643
    • (1997) J. Mol. Biol. , vol.269 , Issue.4 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 27
    • 0036931447 scopus 로고    scopus 로고
    • Toward the physical basis of thermophilic proteins: Linking of enriched polar interactions and reduced heat capacity of unfolding
    • Zhou, H.-X. Toward the physical basis of thermophilic proteins: linking of enriched polar interactions and reduced heat capacity of unfolding Biophys. J. 2002, 83 (6) 3126-3133
    • (2002) Biophys. J. , vol.83 , Issue.6 , pp. 3126-3133
    • Zhou, H.-X.1
  • 28
    • 0030043489 scopus 로고    scopus 로고
    • Cation-π interactions in chemistry and biology: A new view of benzene, Phe, Tyr and Typ
    • Dougherty, D. Cation-π interactions in chemistry and biology: a new view of benzene, Phe, Tyr and Typ Science 1996, 271 (5246) 163-168
    • (1996) Science , vol.271 , Issue.5246 , pp. 163-168
    • Dougherty, D.1
  • 29
    • 0036425552 scopus 로고    scopus 로고
    • Role of cation-pi interactions to the stability of thermophilic proteins
    • Gromiha, M. M.; Thomas, S.; Santosh, C. Role of cation-pi interactions to the stability of thermophilic proteins Prep. Biochem. Biotehnol. 2002, 32 (4) 355-62
    • (2002) Prep. Biochem. Biotehnol. , vol.32 , Issue.4 , pp. 355-362
    • Gromiha, M.M.1    Thomas, S.2    Santosh, C.3
  • 30
    • 24644472817 scopus 로고    scopus 로고
    • Physics and evolution of thermophiles adaptation
    • Berezovsky, I. N.; Shakhnovich, E. I. Physics and evolution of thermophiles adaptation Proc. Natl. Acad. Sci. U.S.A. 2005, 102 (36) 12742-12747
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , Issue.36 , pp. 12742-12747
    • Berezovsky, I.N.1    Shakhnovich, E.I.2
  • 31
    • 79952487469 scopus 로고    scopus 로고
    • Protein rigidity and thermophilic adaptation
    • Radestock, S.; Gohlke, H. Protein rigidity and thermophilic adaptation Proteins 2011, 79 (4) 1089-1108
    • (2011) Proteins , vol.79 , Issue.4 , pp. 1089-1108
    • Radestock, S.1    Gohlke, H.2
  • 32
    • 0034654087 scopus 로고    scopus 로고
    • Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermatoga maritima
    • Thoma, R.; Henning, M.; Sterner, R.; Kirschner, K. Structure and function of mutationally generated monomers of dimeric phosphoribosylanthranilate isomerase from Thermatoga maritima Structure 2000, 8 (3) 265-276
    • (2000) Structure , vol.8 , Issue.3 , pp. 265-276
    • Thoma, R.1    Henning, M.2    Sterner, R.3    Kirschner, K.4
  • 33
    • 80052449370 scopus 로고    scopus 로고
    • How do thermophilic proteins and proteomes withstand high temperature
    • Sawle, L.; Ghosh, K. How do thermophilic proteins and proteomes withstand high temperature Biophys. J. 2011, 101 (1) 217-227
    • (2011) Biophys. J. , vol.101 , Issue.1 , pp. 217-227
    • Sawle, L.1    Ghosh, K.2
  • 34
    • 0017706821 scopus 로고
    • Reversible thermal unfolding of thermostable phosphoglycerate kinase. Thermostability associated with mean zero enthalpy change
    • Nojima, H.; Ikai, A.; Oshima, T.; Noda, H. Reversible thermal unfolding of thermostable phosphoglycerate kinase. Thermostability associated with mean zero enthalpy change J. Mol. Biol. 1977, 116 (3) 429-442
    • (1977) J. Mol. Biol. , vol.116 , Issue.3 , pp. 429-442
    • Nojima, H.1    Ikai, A.2    Oshima, T.3    Noda, H.4
  • 35
    • 78649674883 scopus 로고    scopus 로고
    • Protein heat capacity: An anomaly that maybe never was
    • Cooper, A. Protein heat capacity: an anomaly that maybe never was J. Phys. Chem. Lett. 2010, 1 (22) 3298-3304
    • (2010) J. Phys. Chem. Lett. , vol.1 , Issue.22 , pp. 3298-3304
    • Cooper, A.1
  • 36
    • 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 (5) 1665-1676
    • (2012) Chem. Soc. Rev. , vol.41 , Issue.5 , pp. 1665-1676
    • Sterpone, F.1    Melchionna, S.2
  • 38
    • 0027333483 scopus 로고
    • Differential stability of beta-sheets and alpha-helices in beta-lactamase: A high temperature molecular dynamics study of unfolding intermediates
    • Vijayakumar, S.; Vishveshwara, S.; Ravishanker, G.; Beveridge, D. L. Differential stability of beta-sheets and alpha-helices in beta-lactamase: a high temperature molecular dynamics study of unfolding intermediates Biophys. J. 1993, 65 (6) 2304-2312
    • (1993) Biophys. J. , vol.65 , Issue.6 , pp. 2304-2312
    • Vijayakumar, S.1    Vishveshwara, S.2    Ravishanker, G.3    Beveridge, D.L.4
  • 40
    • 61749089197 scopus 로고    scopus 로고
    • Key role of proximal water in regulating thermostable proteins
    • Sterpone, F.; Bertonati, C.; Briganti, G.; Melchionna, S. Key role of proximal water in regulating thermostable proteins J. Phys. Chem. B 2009, 113 (1) 131-137
    • (2009) J. Phys. Chem. B , vol.113 , Issue.1 , pp. 131-137
    • Sterpone, F.1    Bertonati, C.2    Briganti, G.3    Melchionna, S.4
  • 41
    • 34547485422 scopus 로고    scopus 로고
    • How protein surface induce anomalous dynamics of hydration water
    • Pizzitutti, F.; Marchi, M.; Sterpone, F.; Rossky, P. J. How protein surface induce anomalous dynamics of hydration water J. Phys. Chem. B 2007, 111 (26) 7584-7590
    • (2007) J. Phys. Chem. B , vol.111 , Issue.26 , pp. 7584-7590
    • Pizzitutti, F.1    Marchi, M.2    Sterpone, F.3    Rossky, P.J.4
  • 42
    • 79959369421 scopus 로고    scopus 로고
    • Molecular basis of the thermostability and thermophilicity of laminarinases: X-ray structure of the hyperthermostable laminarinase from Rhodothermus marinus and molecular dynamics simulations
    • Bleicher, L.; Prates, E. T.; Gomes, T. C.; Silveira, R. L.; Nascimento, A. S.; Rojas, A. L.; Golubev, A.; Martínez, L.; Skaf, M. S.; Polikarpov, I. Molecular basis of the thermostability and thermophilicity of laminarinases: X-ray structure of the hyperthermostable laminarinase from Rhodothermus marinus and molecular dynamics simulations J. Phys. Chem. B 2011, 115 (24) 7940-7949
    • (2011) J. Phys. Chem. B , vol.115 , Issue.24 , pp. 7940-7949
    • Bleicher, L.1    Prates, E.T.2    Gomes, T.C.3    Silveira, R.L.4    Nascimento, A.S.5    Rojas, A.L.6    Golubev, A.7    Martínez, L.8    Skaf, M.S.9    Polikarpov, I.10
  • 43
    • 0002353040 scopus 로고
    • Temperature adaptation of enzymes: Biological optimization through structure-function compromises
    • Somero, G. N. Temperature adaptation of enzymes: biological optimization through structure-function compromises Annu. Rev. Ecol. Syst. 1978, 9, 1-29
    • (1978) Annu. Rev. Ecol. Syst. , vol.9 , pp. 1-29
    • Somero, G.N.1
  • 44
    • 79952487469 scopus 로고    scopus 로고
    • Protein rigidity and thermophilic adaptation
    • Radestock, S.; Gohlke, H. Protein rigidity and thermophilic adaptation Proteins 2011, 79 (4) 1089-1108
    • (2011) Proteins , vol.79 , Issue.4 , pp. 1089-1108
    • Radestock, S.1    Gohlke, H.2
  • 45
    • 0032521456 scopus 로고    scopus 로고
    • The structure of SAICAR synthetase: An enzyme in the de novo pathway of purine nucleotide biosynthesis
    • Levdikov, V. M.; Barynin, V. V.; Grebenko, A. I.; Melik-Adamyan, W. R.; Lamzin, V. S.; Wilson, K. S. The structure of SAICAR synthetase: an enzyme in the de novo pathway of purine nucleotide biosynthesis Structure 1998, 6 (3) 363-376
    • (1998) Structure , vol.6 , Issue.3 , pp. 363-376
    • Levdikov, V.M.1    Barynin, V.V.2    Grebenko, A.I.3    Melik-Adamyan, W.R.4    Lamzin, V.S.5    Wilson, K.S.6
  • 46
    • 33746338273 scopus 로고    scopus 로고
    • Nucleotide complexes of Escherichia coli phosphoribosylaminoimidazole succinocarboxamide synthetase
    • Ginder, N. D.; Binkowski, D. J.; Fromm, H. J.; Honzatko, R. B. Nucleotide complexes of Escherichia coli phosphoribosylaminoimidazole succinocarboxamide synthetase J. Biol. Chem. 2006, 281 (30) 20680-20688
    • (2006) J. Biol. Chem. , vol.281 , Issue.30 , pp. 20680-20688
    • Ginder, N.D.1    Binkowski, D.J.2    Fromm, H.J.3    Honzatko, R.B.4
  • 47
  • 49
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL Workspace: A web-based environment for protein structure homology modelling
    • Arnold, K.; Bordoli, L.; Kopp, J.; Schwede, T. The SWISS-MODEL Workspace: a web-based environment for protein structure homology modelling Bioinformatics 2006, 22 (2) 195-201
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 51
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B.; Kutzner, C.; van der Spoel, D.; Lindahl, E. GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation J. Chem. Theory Comput. 2008, 4 (3) 435-447
    • (2008) J. Chem. Theory Comput. , vol.4 , Issue.3 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 52
    • 33645941402 scopus 로고
    • The OPLS [optimized potentials for liquid simulations] potential functions for proteins, energy minimization for crystals of cyclic peptides and crambin
    • Jorgensen, W. L.; Tirado-Rives, J. The OPLS [optimized potentials for liquid simulations] potential functions for proteins, energy minimization for crystals of cyclic peptides and crambin J. Am. Chem. Soc. 1988, 110 (6) 1657-1666
    • (1988) J. Am. Chem. Soc. , vol.110 , Issue.6 , pp. 1657-1666
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 54
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N log(N) method for sums in large systems
    • Darden, T.; York, D.; Pederesen, L. Particle mesh Ewald: an N.log(N) method for sums in large systems J. Chem. Phys. 1993, 98 (12) 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , Issue.12 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pederesen, L.3
  • 55
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • Hess, B.; Bekker, H.; Berendsen, H. J. C.; Fraaije, J. G. E. M. LINCS: a linear constraint solver for molecular simulations J. Comput. Chem. 1997, 18 (12) 1463-1472
    • (1997) J. Comput. Chem. , vol.18 , Issue.12 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.J.C.3    Fraaije, J.G.E.M.4
  • 56
    • 34547809547 scopus 로고
    • A unified formulation of the constant temperature molecular-dynamics methods
    • Nose, S. A unified formulation of the constant temperature molecular-dynamics methods J. Chem. Phys. 1984, 81 (1) 511-519
    • (1984) J. Chem. Phys. , vol.81 , Issue.1 , pp. 511-519
    • Nose, S.1
  • 57
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • Hoover, W. G. Canonical dynamics: equilibrium phase-space distributions Phys. Rev. A 1985, 31 (3) 1695-1697
    • (1985) Phys. Rev. A , vol.31 , Issue.3 , pp. 1695-1697
    • Hoover, W.G.1
  • 58
    • 0019707626 scopus 로고
    • Polymorphic transitions in single crystals: A new molecular dynamics method
    • Parrinello, M.; Rahman, A. Polymorphic transitions in single crystals: a new molecular dynamics method J. Appl. Phys. 1981, 52 (12) 7182-7190
    • (1981) J. Appl. Phys. , vol.52 , Issue.12 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 60
    • 33746218852 scopus 로고    scopus 로고
    • MUSTANG: A multiple structural alignment algorithm
    • Konagurthu, A. S.; Whisstock, J. C.; Stuckey, P. J.; Lesk, A. M. MUSTANG: a multiple structural alignment algorithm Proteins 2006, 64 (3) 559-574
    • (2006) Proteins , vol.64 , Issue.3 , pp. 559-574
    • Konagurthu, A.S.1    Whisstock, J.C.2    Stuckey, P.J.3    Lesk, A.M.4
  • 61
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W.; Sander, C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Biopolymers 1983, 22 (12) 2577-2637
    • (1983) Biopolymers , vol.22 , Issue.12 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 62
    • 0029361842 scopus 로고
    • Relationship of sidechain hydrophobicity and α-helical propensity on the stability of single-stranded amphipathic α-helix
    • Monera, O. D.; Sereda, T. J.; Zhou, N. E.; Kay, C. M.; Hodges, R. S. Relationship of sidechain hydrophobicity and α-helical propensity on the stability of single-stranded amphipathic α-helix J. Pept. Sci. 1995, 1 (5) 319-329
    • (1995) J. Pept. Sci. , vol.1 , Issue.5 , pp. 319-329
    • Monera, O.D.1    Sereda, T.J.2    Zhou, N.E.3    Kay, C.M.4    Hodges, R.S.5
  • 63
    • 84858320073 scopus 로고    scopus 로고
    • Dynamic fingerprints of protein thermostability revealed by long molecular dynamics
    • Marcos, E.; Jiménez, A.; Crehuet, Ramon 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    Jiménez, A.2    Ramon, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.