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Volumn 78, Issue 1, 2000, Pages 416-429

A thermodynamic molecular switch in biological systems: Ribonuclease S' fragment complementation reactions

Author keywords

[No Author keywords available]

Indexed keywords

RIBONUCLEASE;

EID: 0034033142     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76604-5     Document Type: Article
Times cited : (17)

References (36)
  • 2
    • 0015214585 scopus 로고
    • Thermodynamics, chemical reactions, and molecular biology
    • T.H. Benzinger Thermodynamics, chemical reactions, and molecular biology Nature 200 1971 100 103
    • (1971) Nature , vol.200 , pp. 100-103
    • Benzinger, T.H.1
  • 3
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: a mechanism of protein structure stabilization
    • S.K. Burley G.A. Petsko Aromatic-aromatic interaction: a mechanism of protein structure stabilization Science 229 1985 23 38
    • (1985) Science , vol.229 , pp. 23-38
    • Burley, S.K.1    Petsko, G.A.2
  • 4
    • 85120146260 scopus 로고    scopus 로고
    • Chase, M. W., Jr., C. A. Davies, J. K. Downey, D. J. Frurip, R. A. McDonald, and A. N. Syverud. 1985. JANAF Thermodynamic Tables, 3rd ed., Vol. 14, Part II. ACS and the American Institute of Physics for the National Bureau of Standards, Washington, D.C.
  • 5
    • 84990677036 scopus 로고
    • Approximation of the Planck-Benzinger thermal work function in protein refolding in ribonuclease systems
    • P.W. Chun Approximation of the Planck-Benzinger thermal work function in protein refolding in ribonuclease systems Int. J. Quantum Chem. Quantum Biol. Symp. 15 1988 247 258
    • (1988) Int. J. Quantum Chem. Quantum Biol. Symp. , vol.15 , pp. 247-258
    • Chun, P.W.1
  • 6
    • 0003923391 scopus 로고
    • Manual for Computer-Aided Analysis of Biochemical Proc. R. Soc. London Ser. Aesses with Florida 1-2-4
    • P.W. Chun Manual for Computer-Aided Analysis of Biochemical Proc. R. Soc. London Ser. Aesses with Florida 1-2-4 1991 University of Florida Gainesville, FL
    • (1991)
    • Chun, P.W.1
  • 7
    • 33751157340 scopus 로고
    • The Planck-Benzinger thermal work function: definition of temperature-invariant enthalpy in biological systems
    • P.W. Chun The Planck-Benzinger thermal work function: definition of temperature-invariant enthalpy in biological systems J. Phys. Chem. 86 1994 6851 6861
    • (1994) J. Phys. Chem. , vol.86 , pp. 6851-6861
    • Chun, P.W.1
  • 8
    • 0029063675 scopus 로고
    • New thermodynamic studies on ribonuclease A at low pH
    • P.W. Chun New thermodynamic studies on ribonuclease A at low pH J. Biol. Chem. 270 1995 13925 13931
    • (1995) J. Biol. Chem. , vol.270 , pp. 13925-13931
    • Chun, P.W.1
  • 9
    • 85120117530 scopus 로고    scopus 로고
    • New thermodynamic studies on hydrogen bond energy of liquid water
    • P.W. Chun New thermodynamic studies on hydrogen bond energy of liquid water American Chemical Society, Biophysical Chemistry, poster 283, 212th national American Chemistry Society Meeting Orlando, FL 1996
    • (1996)
    • Chun, P.W.1
  • 10
    • 0001396886 scopus 로고    scopus 로고
    • The Planck-Benzinger thermal work function: determination of the thermodynamic stability of chymotrypsinogen A and ribonuclease A in glycerol
    • P.W. Chun The Planck-Benzinger thermal work function: determination of the thermodynamic stability of chymotrypsinogen A and ribonuclease A in glycerol J. Phys. Chem. 100 1996 7283 7292
    • (1996) J. Phys. Chem. , vol.100 , pp. 7283-7292
    • Chun, P.W.1
  • 11
    • 0031235347 scopus 로고    scopus 로고
    • Planck-Benzinger thermal work function: thermodynamic approach to site-specific S-protein and S-peptides interactions in the ribonuclease S′ system
    • P.W. Chun Planck-Benzinger thermal work function: thermodynamic approach to site-specific S-protein and S-peptides interactions in the ribonuclease S′ system J. Phys. Chem. B 101 1997 7835 7843
    • (1997) J. Phys. Chem. B , vol.101 , pp. 7835-7843
    • Chun, P.W.1
  • 12
    • 85120146982 scopus 로고    scopus 로고
    • A thermodynamic approach to the unfolding of wild-type R96 and temperature-sensitive mutant R96H (Arg → His), Poster W411
    • P.W. Chun A thermodynamic approach to the unfolding of wild-type R96 and temperature-sensitive mutant R96H (Arg → His), Poster W411 Biophysical Chemistry, 213th national ACS Meeting San Francisco, California 1997
    • (1997)
    • Chun, P.W.1
  • 13
    • 0032317158 scopus 로고    scopus 로고
    • Application of Planck-Benzinger relationships to biology
    • P.W. Chun Application of Planck-Benzinger relationships to biology Methods Enzymol. 295 1998 227 268
    • (1998) Methods Enzymol. , vol.295 , pp. 227-268
    • Chun, P.W.1
  • 14
    • 85120129119 scopus 로고    scopus 로고
    • Chun, P. W. 1999. Uncovering the innate thermodynamic quantities in protein unfolding. Int. J. Quantum Chem. Sanibel Symp. (in press).
  • 16
    • 0025801444 scopus 로고
    • A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme
    • P. Connelly L. Ghosaini C.-Q. Hu A. Kitamura J.M. Sturtevant A differential scanning calorimetric study of the thermal unfolding of seven mutant forms of phage T4 lysozyme Biochemistry 30 1991 1887 1891
    • (1991) Biochemistry , vol.30 , pp. 1887-1891
    • Connelly, P.1    Ghosaini, L.2    Hu, C.-Q.3    Kitamura, A.4    Sturtevant, J.M.5
  • 17
    • 0025293251 scopus 로고
    • Thermodynamics of protein-protein interactions in the ribonuclease S system studied by titration calorimetry
    • P. Connelly R. Varadarajan J.M. Sturtevant F.M. Richards Thermodynamics of protein-protein interactions in the ribonuclease S system studied by titration calorimetry Biochemistry 29 1990 6108 6114
    • (1990) Biochemistry , vol.29 , pp. 6108-6114
    • Connelly, P.1    Varadarajan, R.2    Sturtevant, J.M.3    Richards, F.M.4
  • 18
    • 0004005645 scopus 로고
    • The Strength of Chemical Bonds
    • T.L. Cottrell The Strength of Chemical Bonds 1958 Academic Press New York and London 21–70
    • (1958)
    • Cottrell, T.L.1
  • 20
    • 0000762110 scopus 로고
    • The calculation of free energy from spectroscopic data
    • W.F. Giauque The calculation of free energy from spectroscopic data J. Am. Chem. Soc. 52 1930 4808 4815
    • (1930) J. Am. Chem. Soc. , vol.52 , pp. 4808-4815
    • Giauque, W.F.1
  • 21
    • 0000729128 scopus 로고
    • The entropy of hydrogen and the third law of thermodynamics, the free energy and dissociation of hydrogen
    • W.F. Giauque The entropy of hydrogen and the third law of thermodynamics, the free energy and dissociation of hydrogen J. Am. Chem. Soc. 52 1930 4816 4831
    • (1930) J. Am. Chem. Soc. , vol.52 , pp. 4816-4831
    • Giauque, W.F.1
  • 22
    • 33947353589 scopus 로고
    • Hydrogen sulfide, the heat capacity and vapor pressure of solid and liquid, the heat of vaporization, a comparison of thermodynamic and spectroscopic values of the entropy
    • W.F. Giauque R.W. Blue Hydrogen sulfide, the heat capacity and vapor pressure of solid and liquid, the heat of vaporization, a comparison of thermodynamic and spectroscopic values of the entropy J. Am. Chem. Soc. 58 1930 831 837
    • (1930) J. Am. Chem. Soc. , vol.58 , pp. 831-837
    • Giauque, W.F.1    Blue, R.W.2
  • 23
    • 0001805804 scopus 로고
    • Entropies of N2O4 and NO2. Heat capacities from 15K to B.P. Heat of vaporization and the vapor pressure-equilibrium N2O4=2NO2=2NO+O2
    • 2 J. Chem. Phys. 6 1938 40 52[[page end]]
    • (1938) J. Chem. Phys. , vol.6 , pp. 40-52[[page end]]
    • Giauque, W.F.1    Kemp, J.D.2
  • 24
    • 0000671699 scopus 로고
    • The heat capacities and entropies of aluminum and copper from 15 to 300K
    • W.F. Giauque P.F. Meads The heat capacities and entropies of aluminum and copper from 15 to 300 K J. Am. Chem. Soc. 63 1941 1897 1901
    • (1941) J. Am. Chem. Soc. , vol.63 , pp. 1897-1901
    • Giauque, W.F.1    Meads, P.F.2
  • 25
    • 0010084188 scopus 로고
    • On the equilibrium of heterogeneous substance
    • J.W. Gibbs On the equilibrium of heterogeneous substance Am. J. Sci. 3 series 16 1878 441 458 (via Trans. Conn. Acad. Sci. 3:228–232)
    • (1878) Am. J. Sci. 3 series , vol.16 , pp. 441-458
    • Gibbs, J.W.1
  • 26
    • 85120106499 scopus 로고
    • Thermodynamics of the binding of S-peptide to S-protein to form ribonuclease S′
    • R.P. Hearn F.M. Richards J.M. Sturtevant G.D. Watt Thermodynamics of the binding of S-peptide to S-protein to form ribonuclease S′ Biochemistry 30 1971 1887 1891
    • (1971) Biochemistry , vol.30 , pp. 1887-1891
    • Hearn, R.P.1    Richards, F.M.2    Sturtevant, J.M.3    Watt, G.D.4
  • 27
    • 0031213481 scopus 로고    scopus 로고
    • Determining temperature-invariant enthalpy change and other thermodynamic functions on transformation of proteins and other biopolymers
    • J.P. Johari Determining temperature-invariant enthalpy change and other thermodynamic functions on transformation of proteins and other biopolymers J. Phys. Chem. B 101 1997 6780 6785
    • (1997) J. Phys. Chem. B , vol.101 , pp. 6780-6785
    • Johari, J.P.1
  • 28
    • 0024535615 scopus 로고    scopus 로고
    • A scanning calorimetric study of the denaturation of the lysozyme phage T4 and Arg → His mutant form thereof
    • S. Kitamura J.M. Sturtevant A scanning calorimetric study of the denaturation of the lysozyme phage T4 and Arg → His mutant form thereof Biochemistry 28 1998 3788 3792
    • (1998) Biochemistry , vol.28 , pp. 3788-3792
    • Kitamura, S.1    Sturtevant, J.M.2
  • 29
    • 85120137167 scopus 로고
    • G.N. Lewis M. Randall K.S. Pitzer L. Brewer Thermodynamics 1961 McGraw-Hill New York 164 182 665–668
    • (1961) , pp. 164-182
    • Lewis, G.N.1    Randall, M.2
  • 30
    • 0003466967 scopus 로고
    • Physical Chemistry
    • E.A. Moelwyn-Hughes Physical Chemistry 1957 Pergamon Press New York 90–103, 264–279, 560–563
    • (1957)
    • Moelwyn-Hughes, E.A.1
  • 32
    • 24544464348 scopus 로고
    • Structure of water and hydrophobic bonding in proteins. I. A model for the thermodynamic properties of liquid water
    • G. Nemethy H.A. Scheraga Structure of water and hydrophobic bonding in proteins. I. A model for the thermodynamic properties of liquid water J. Chem. Phys. 36 1962 3382 3400
    • (1962) J. Chem. Phys. , vol.36 , pp. 3382-3400
    • Nemethy, G.1    Scheraga, H.A.2
  • 33
    • 0004014513 scopus 로고
    • Treatise on Thermodynamics
    • M. Planck Treatise on Thermodynamics 7th ed. 1927 A. Ogg, translator. Longmans, Green and Co London 164–182, 665–668
    • (1927)
    • Planck, M.1
  • 34
    • 0141617765 scopus 로고
    • Quantum thermodynamics: the microscopic basis of entropy and linear thermodynamic relations
    • W. Rhodes Quantum thermodynamics: the microscopic basis of entropy and linear thermodynamic relations J. Phys. Chem. 95 1991 10246 10252
    • (1991) J. Phys. Chem. , vol.95 , pp. 10246-10252
    • Rhodes, W.1
  • 35
    • 0003534782 scopus 로고
    • Circular of the National Bureau of Standards 500, Related Values of Chemical Thermodynamic Properties
    • F.D. Rossini D.D. Wagnman Circular of the National Bureau of Standards 500, Related Values of Chemical Thermodynamic Properties 1952 U.S. Government Printing Office Washington, DC.
    • (1952)
    • Rossini, F.D.1    Wagnman, D.D.2
  • 36
    • 0026582848 scopus 로고
    • Heat capacity changes for protein-peptide interactions in the ribonuclease S′ system
    • R. Varadarajan P.R. Connelly J.M. Sturtevant F.M. Richards Heat capacity changes for protein-peptide interactions in the ribonuclease S′ system Biochemistry 31 1992 1421 1426
    • (1992) Biochemistry , vol.31 , pp. 1421-1426
    • Varadarajan, R.1    Connelly, P.R.2    Sturtevant, J.M.3    Richards, F.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.