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Volumn 109, Issue 38, 2005, Pages 18184-18188

Favorable entropy of aromatic clusters in thermophilic proteins

Author keywords

[No Author keywords available]

Indexed keywords

ENTROPY; FREE ENERGY; OSCILLATIONS; PROTEINS;

EID: 26844433039     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp052333u     Document Type: Article
Times cited : (5)

References (21)
  • 1
    • 0039116206 scopus 로고    scopus 로고
    • Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: Results of a comprehensive survey
    • Szilagyi, A.; Zavodszky, 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
    • Szilagyi, A.1    Zavodszky, P.2
  • 2
    • 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, 3126-3133.
    • (2002) Biophys. J. , vol.83 , pp. 3126-3133
    • Zhou, H.-X.1
  • 3
    • 0031614960 scopus 로고    scopus 로고
    • Proteins from hyperthermophiles: Stability and enzymic catalysis close to the boiling point of water
    • Biotechnology of Extremophiles
    • Ladenstein, R.; Antranikian, G. Proteins from hyperthermophiles: Stability and enzymic catalysis close to the boiling point of water. Adv. Biochem. Eng./Blotechnol. 1998, 61, 37-85 (Biotechnology of Extremophiles).
    • (1998) Adv. Biochem. Eng./Blotechnol. , vol.61 , pp. 37-85
    • Ladenstein, R.1    Antranikian, G.2
  • 4
    • 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
  • 6
    • 0031280508 scopus 로고    scopus 로고
    • Thermophilic proteins: Stability and function in aqueous and organic solvents
    • Cowan, D. A. Thermophilic proteins: Stability and function in aqueous and organic solvents. Comp. Biochem. Physiol., Part A: Mol. Integr. Physiol. 1997, 118, 429-438.
    • (1997) Comp. Biochem. Physiol., Part A: Mol. Integr. Physiol. , vol.118 , pp. 429-438
    • Cowan, D.A.1
  • 7
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • 1998
    • Jaenicke, R.; Bohm, G. 1998, The stability of proteins in extreme environments. Curr. Opin. Struct. Biol. 1998, 8, 738-748.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 738-748
    • Jaenicke, R.1    Bohm, G.2
  • 8
    • 84986432905 scopus 로고
    • Accurate modeling of the intramolecular electrostatic energy of proteins
    • Dudek, M. J.; Ponder, J. W. Accurate modeling of the intramolecular electrostatic energy of proteins. J. Comput. Chem. 1995, 16, 791-816.
    • (1995) J. Comput. Chem. , vol.16 , pp. 791-816
    • Dudek, M.J.1    Ponder, J.W.2
  • 9
    • 84986533794 scopus 로고
    • Algorithms for calculating excluded volume and its derivatives as a function of molecular conformation and their use in energy minimization
    • Kundrot, C. E.; Ponder, J. W.; Richards, F. M. Algorithms for calculating excluded volume and its derivatives as a function of molecular conformation and their use in energy minimization. J. Comput. Chem. 1991, 12, 402-409.
    • (1991) J. Comput. Chem. , vol.12 , pp. 402-409
    • Kundrot, C.E.1    Ponder, J.W.2    Richards, F.M.3
  • 10
    • 84988112508 scopus 로고
    • An efficient Newton-like method for molecular mechanics energy minimization of large molecules
    • Ponder, J. W.; Richards, F. M. An efficient Newton-like method for molecular mechanics energy minimization of large molecules. J. Comput. Chem. 1987, 8, 1016.
    • (1987) J. Comput. Chem. , vol.8 , pp. 1016
    • Ponder, J.W.1    Richards, F.M.2
  • 11
    • 14844346946 scopus 로고    scopus 로고
    • Intraresidue distribution of energy in proteins
    • Trebbi, B.; Fanti, M.; Rossi, I.; Zerbetto, F. Intraresidue distribution of energy in proteins. J. Phys. Chem. B 2005, 109, 3586-3593.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 3586-3593
    • Trebbi, B.1    Fanti, M.2    Rossi, I.3    Zerbetto, F.4
  • 13
    • 0842341831 scopus 로고    scopus 로고
    • The effect of guest inclusion on the crystal packing of p-tert-butylcalix[4]arenas
    • León, S.; Leigh, D. A.; Zerbetto, F. The effect of guest inclusion on the crystal packing of p-tert-butylcalix[4]arenas. Chem.-Eur. J. 2002, 8, 4854-4866.
    • (2002) Chem.-Eur. J. , vol.8 , pp. 4854-4866
    • León, S.1    Leigh, D.A.2    Zerbetto, F.3
  • 14
    • 0037455133 scopus 로고    scopus 로고
    • On the cavitation energy of water
    • Höfinger, S.; Zerbetto, F. On the cavitation energy of water. Chem.-Eur. J. 2003, 9, 566-569.
    • (2003) Chem.-Eur. J. , vol.9 , pp. 566-569
    • Höfinger, S.1    Zerbetto, F.2
  • 15
    • 0038111016 scopus 로고    scopus 로고
    • Molecular dynamics and implications for the photophysics of a dendrimer-dye guest-host system
    • Teobaldi, G.; Zerbetto, F. Molecular dynamics and implications for the photophysics of a dendrimer-dye guest-host system. J. Am. Chem. Soc. 2003, 125, 7388-7393.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 7388-7393
    • Teobaldi, G.1    Zerbetto, F.2
  • 17
    • 84986525856 scopus 로고
    • A comprehensive study of the rotational energy profiles of organic systems by ab initio MO theory, forming a basis for peptide torsional parameters
    • Maxwell, D. S.; Tirado-Rives, J.; Jorgensen, W. L. A comprehensive study of the rotational energy profiles of organic systems by ab initio MO theory, forming a basis for peptide torsional parameters. J. Comput. Chem. 1985, 16, 984-1010.
    • (1985) J. Comput. Chem. , vol.16 , pp. 984-1010
    • Maxwell, D.S.1    Tirado-Rives, J.2    Jorgensen, W.L.3
  • 18
    • 0001351515 scopus 로고
    • Estimation of absolute and relative entropies of macromolecules using the covariance matrix
    • Schlitter, J. Estimation of absolute and relative entropies of macromolecules using the covariance matrix. Chem. Phys. Lett. 1993, 215, 617-621.
    • (1993) Chem. Phys. Lett. , vol.215 , pp. 617-621
    • Schlitter, J.1
  • 19
    • 0034323089 scopus 로고    scopus 로고
    • Absolute entropies from molecular dynamics simulation trajectories
    • Schäfer, H.; Mark, A. E.; van Gunsteren, W. F. Absolute entropies from molecular dynamics simulation trajectories. J. Chem. Phys. 2000, 113, 7809-7817.
    • (2000) J. Chem. Phys. , vol.113 , pp. 7809-7817
    • Schäfer, H.1    Mark, A.E.2    Van Gunsteren, W.F.3
  • 20
    • 0035314075 scopus 로고    scopus 로고
    • Entropy calculations on a reversibly folding peptide: Changes in solute free energy cannot explain folding behavior
    • Schäfer, H.; Daura, X.; Mark, A. E.; van Gunsteren, W. F. Entropy calculations on a reversibly folding peptide: Changes in solute free energy cannot explain folding behavior. Proteins: Struct., Funct., Genet. 2001, 43, 45-56.
    • (2001) Proteins: Struct., Funct., Genet. , vol.43 , pp. 45-56
    • Schäfer, H.1    Daura, X.2    Mark, A.E.3    Van Gunsteren, W.F.4
  • 21
    • 0036463713 scopus 로고    scopus 로고
    • Increased frequency of cysteine, tyrosine, and phenylalanine residues since the last universal ancestor
    • Brooks, D. J.; Fresco, J. R. Increased frequency of cysteine, tyrosine, and phenylalanine residues since the last universal ancestor. Mol. Cell. Proteomics 2002, 1, 125-131.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 125-131
    • Brooks, D.J.1    Fresco, J.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.