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Volumn 250, Issue 5, 1995, Pages 689-694

Thermodynamics of unfolding of ribonuclease a under high pressure. A study by proton NMR

Author keywords

High pressure; NMR; Protein unfolding; Ribonuclease A; Thermodynamics

Indexed keywords

RIBONUCLEASE A;

EID: 0029143128     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1995.0408     Document Type: Article
Times cited : (68)

References (21)
  • 1
    • 0026160291 scopus 로고
    • Temperature-jump NMR study of protein folding: Ribonuclease A at low pH
    • Akasaka, K., Naito, A. & Nakatani, H. (1991).Temperature-jump NMR study of protein folding: ribonuclease A at low pH. J. Biomol. NMR, 1, 65-70.
    • (1991) J. Biomol. NMR , vol.1 , pp. 65-70
    • Akasaka, K.1    Naito, A.2    Nakatani, H.3
  • 2
    • 0014952474 scopus 로고
    • Thermodynamics of protein denaturation. Effect of pressure on the denaturation of ribonuclease A
    • Brandts, J. F., Oliveira, R. J. & Westort, C. (1970). Thermodynamics of protein denaturation. Effect of pressure on the denaturation of ribonuclease A. Biochemistry, 9, 1038-1047.
    • (1970) Biochemistry , vol.9 , pp. 1038-1047
    • Brandts, J.F.1    Oliveira, R.J.2    Westort, C.3
  • 3
    • 0015236387 scopus 로고
    • Reversible pressure to temperature denaturation of chymotripsinogen
    • Hawley SA. (1971). Reversible pressure to temperature denaturation of chymotripsinogen. Biochemistry, 10, 2436-2442.
    • (1971) Biochemistry , vol.10 , pp. 2436-2442
    • Hawley, S.A.1
  • 4
    • 0001016335 scopus 로고
    • Nuclear magnetic resonance measurements at high pressure
    • Jonas, J. (1972). Nuclear magnetic resonance measurements at high pressure. Rev. Sci. Instrum. 43, 643-649.
    • (1972) Rev. Sci. Instrum. , vol.43 , pp. 643-649
    • Jonas, J.1
  • 5
    • 0008863560 scopus 로고
    • Some factors in the interaction of protein denaturation
    • Kauzmann, W. (1959). Some factors in the interaction of protein denaturation. Advan. Protein Chem. 14, 1-63.
    • (1959) Advan. Protein Chem. , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 7
    • 0017054059 scopus 로고
    • Plurality of pressure to denatured forms in chymotripsinogen and lysozyme
    • Li, T. M., Hook, J. M., III, Drickamer, H. G. & Weber, G. (1976). Plurality of pressure to denatured forms in chymotripsinogen and lysozyme. Biochemistry, 15, 5571-5580.
    • (1976) Biochemistry , vol.15 , pp. 5571-5580
    • Li, T.M.1    Hook, J.M.2    Drickamer, H.G.3    Weber, G.4
  • 8
    • 0021106295 scopus 로고
    • High-pressure nuclear magnetic resonance studies ofhemeproteins. Pressure to induced structural changes in the heme environments of ferric low to spin metmyoglobin complexes
    • Morishima, I. & Hara, M. (1983). High-pressure nuclear magnetic resonance studies ofhemeproteins. Pressure to induced structural changes in the heme environments of ferric low to spin metmyoglobin complexes. Biochemistry, 22, 4102-4107.
    • (1983) Biochemistry , vol.22 , pp. 4102-4107
    • Morishima, I.1    Hara, M.2
  • 9
    • 0028058671 scopus 로고
    • High-pressure study of the dissociation of Arc repressor
    • Peng, X. & Jonas, J. (1994). High-pressure study of the dissociation of Arc repressor. Biochemistry, 33, 8323-8329.
    • (1994) Biochemistry , vol.33 , pp. 8323-8329
    • Peng, X.1    Jonas, J.2
  • 10
    • 0018588511 scopus 로고
    • Stability of proteins. Small globular proteins
    • Privalov, P. L. (1979). Stability of proteins. Small globular proteins. Advan. Protein Chem. 33, 167-241.
    • (1979) Advan. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 11
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interaction
    • Privalov, P. L. & Gill, S. J. (1989). Stability of protein structure and hydrophobic interaction. Advan. Protein Chem. 39, 191-234.
    • (1989) Advan. Protein Chem. , vol.39 , pp. 191-234
    • Privalov, P.L.1    Gill, S.J.2
  • 12
    • 0025287103 scopus 로고
    • Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: Protein unfolding effects
    • Privalov, P. L. & Makhatadze, G. I. (1990). Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: Protein unfolding effects. J. Mol. Biol. 213, 385-391.
    • (1990) J. Mol. Biol. , vol.213 , pp. 385-391
    • Privalov, P.L.1    Makhatadze, G.I.2
  • 13
    • 0027180821 scopus 로고
    • Effects of amino acid substitution on the pressure denaturation of staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy
    • Royer, C. A., Hinck, A. P., Loh, S. N. Prehoda, K. E., Peng X., Jonas J. & Markley J. L. (1993). Effects of amino acid substitution on the pressure denaturation of staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy. Biochemistry, 32, 5222-5232.
    • (1993) Biochemistry , vol.32 , pp. 5222-5232
    • Royer, C.A.1    Hinck, A.P.2    Loh Prehoda, S.N.K.E.3    Peng, X.4    Jonas, J.5    Markley, J.L.6
  • 14
    • 0026781884 scopus 로고
    • High-resolution NMR study of the pressure-induced unfolding of lysozyme
    • Samarasinghe, S. D., Campbell, D. M., Jonas, A. & Jonas, J. (1992). High-resolution NMR study of the pressure-induced unfolding of lysozyme. Biochemistry, 31, 7773-7778.
    • (1992) Biochemistry , vol.31 , pp. 7773-7778
    • Samarasinghe, S.D.1    Campbell, D.M.2    Jonas, A.3    Jonas, J.4
  • 15
    • 0342325481 scopus 로고
    • Pressure inactivation of a-chymotripsin
    • Taniguchi, Y. & Suzuki, K. (1983). Pressure inactivation of a-chymotripsin. J. Phys. Chem. 87, 5183-5185.
    • (1983) J. Phys. Chem. , vol.87 , pp. 5183-5185
    • Taniguchi, Y.1    Suzuki, K.2
  • 16
    • 0020791658 scopus 로고
    • H nuclear magnetic resonance titration curves and microenvironments of aromatic residues in bovine pancreatic ribonuclease A
    • Tanokura, M. (1983). 'H nuclear magnetic resonance titration curves and microenvironments of aromatic residues in bovine pancreatic ribonuclease A. J. Biochem. (Tokyo), 94, 51-62.
    • (1983) J. Biochem. (Tokyo) , vol.94 , pp. 51-62
    • Tanokura, M.1
  • 17
    • 3342940544 scopus 로고
    • High resolution NMR measurement under high pressure and pressure dependence of the proton chemical shifts
    • Yamada, H. (1972). High resolution NMR measurement under high pressure and pressure dependence of the proton chemical shifts. Chem. Letters, 747-750.
    • (1972) Chem. Letters , pp. 747-750
    • Yamada, H.1
  • 18
    • 0016056448 scopus 로고
    • Pressure-resisting glass cell for high pressure, high resolution NMR measurement
    • Yamada, H. (1974). Pressure-resisting glass cell for high pressure, high resolution NMR measurement. Rev. Sci. Instrum. 45, 640-642.
    • (1974) Rev. Sci. Instrum. , vol.45 , pp. 640-642
    • Yamada, H.1
  • 19
    • 0002190810 scopus 로고
    • Spinning glass cell for high-pressure high-resolution NMR measurements
    • Yamada, H., Nakatsuka, M., Yamochi, H. & Sawamura, M. (1991). Spinning glass cell for high-pressure high-resolution NMR measurements. Rev. Sci. Instrum. 62, 700-704.
    • (1991) Rev. Sci. Instrum. , vol.62 , pp. 700-704
    • Yamada, H.1    Nakatsuka, M.2    Yamochi, H.3    Sawamura, M.4
  • 21
    • 0015820466 scopus 로고
    • Pressure denaturation of metmyoglobin
    • Zipp, A. & Kauzmann, W. (1973). Pressure denaturation of metmyoglobin. Biochemistry, 12, 4217-4228.
    • (1973) Biochemistry , vol.12 , pp. 4217-4228
    • Zipp, A.1    Kauzmann, W.2


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