메뉴 건너뛰기




Volumn 117, Issue 13, 2013, Pages 3554-3559

Compensating effects of urea and trimethylamine-N-oxide on the heteroassociation of α-chymotrypsin and soybean trypsin inhibitor

Author keywords

[No Author keywords available]

Indexed keywords

EQUILIBRIUM CONSTANTS; METABOLISM; OILSEEDS; THERMOANALYSIS;

EID: 84875794743     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp4006923     Document Type: Article
Times cited : (7)

References (26)
  • 1
    • 0020336190 scopus 로고
    • Living with Water Stress: Evolution of Osmolyte Systems
    • Yancey, P. H.; Clark, M. E.; Hand, S. C.; Bowlus, R. D.; Somero, G. N. Living with Water Stress: Evolution of Osmolyte Systems Science 1982, 217, 1214-1222
    • (1982) Science , vol.217 , pp. 1214-1222
    • Yancey, P.H.1    Clark, M.E.2    Hand, S.C.3    Bowlus, R.D.4    Somero, G.N.5
  • 2
    • 0033428092 scopus 로고    scopus 로고
    • Trimethylamine Oxide Stabilizes Teleost and Mammalian Lactate Dehydrogenases Against Inactivation by Hydrostatic Pressure and Trypsinolysis
    • Yancey, P. H.; Siebenaller, J. F. Trimethylamine Oxide Stabilizes Teleost and Mammalian Lactate Dehydrogenases Against Inactivation by Hydrostatic Pressure and Trypsinolysis J. Exp. Biol. 1999, 202, 3597-3603
    • (1999) J. Exp. Biol. , vol.202 , pp. 3597-3603
    • Yancey, P.H.1    Siebenaller, J.F.2
  • 3
    • 0038290339 scopus 로고    scopus 로고
    • Hydrogen Exchange Kinetics of RNase A and the Urea: TMAO Paradigm
    • Qu, Y.; Bolen, D. W. Hydrogen Exchange Kinetics of RNase A and The Urea: TMAO Paradigm Biochemistry 2003, 42, 5837-5849
    • (2003) Biochemistry , vol.42 , pp. 5837-5849
    • Qu, Y.1    Bolen, D.W.2
  • 4
    • 2342614722 scopus 로고    scopus 로고
    • Counteraction of Urea-induced Protein Denaturation by Trimethylamine N-oxide: A Chemical Chaperone at Atomic Resolution
    • Bennion, B. J.; Daggett, V. Counteraction of Urea-induced Protein Denaturation by Trimethylamine N-oxide: A Chemical Chaperone at Atomic Resolution Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 6433-6438
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 6433-6438
    • Bennion, B.J.1    Daggett, V.2
  • 5
    • 0030805303 scopus 로고    scopus 로고
    • Natural Osmolyte Trimethylamine N-oxide Stimulates Tubulin Polymerization and Reverses Urea Inhibition
    • Sackett, D. L. Natural Osmolyte Trimethylamine N-oxide Stimulates Tubulin Polymerization and Reverses Urea Inhibition Am. J. Physiol. 1997, 273, R669-676
    • (1997) Am. J. Physiol. , vol.273 , pp. 669-676
    • Sackett, D.L.1
  • 7
    • 0035958656 scopus 로고    scopus 로고
    • The Osmophobic Effect: Natural Selection of A Thermodynamic Force in Protein Folding
    • Bolen, D. W.; Baskakov, I. V. The Osmophobic Effect: Natural Selection of A Thermodynamic Force in Protein Folding J. Mol. Biol. 2001, 310, 955-963
    • (2001) J. Mol. Biol. , vol.310 , pp. 955-963
    • Bolen, D.W.1    Baskakov, I.V.2
  • 8
    • 79952835767 scopus 로고    scopus 로고
    • Effect of Nonadditive Repulsive Intermolecular Interactions on the Light Scattering of Concentrated Protein-Osmolyte Mixtures
    • Fernandez, C.; Minton, A. P. Effect of Nonadditive Repulsive Intermolecular Interactions on The Light Scattering of Concentrated Protein-Osmolyte Mixtures J. Phys. Chem. B 2011, 115, 1289-1293
    • (2011) J. Phys. Chem. B , vol.115 , pp. 1289-1293
    • Fernandez, C.1    Minton, A.P.2
  • 9
    • 79960335864 scopus 로고    scopus 로고
    • Modulation of Functionally Significant Conformational Equilibria in Adenylate Kinase by High Concentrations of Trimethylamine Oxide Attributed to Volume Exclusion
    • Nagarajan, S.; Amir, D.; Grupi, A.; Goldenberg, D. P.; Minton, A. P.; Hass, E. Modulation of Functionally Significant Conformational Equilibria in Adenylate Kinase by High Concentrations of Trimethylamine Oxide Attributed to Volume Exclusion Biophys. J. 2011, 100, 2991-2999
    • (2011) Biophys. J. , vol.100 , pp. 2991-2999
    • Nagarajan, S.1    Amir, D.2    Grupi, A.3    Goldenberg, D.P.4    Minton, A.P.5    Hass, E.6
  • 10
    • 0018641198 scopus 로고
    • Counteraction of Urea Destabilization of Protein Structure by Methylamine Osmoregulatory Compounds of Elasmobranch Fishes
    • Yancey, P. H.; Somero, G. N. Counteraction of Urea Destabilization of Protein Structure by Methylamine Osmoregulatory Compounds of Elasmobranch Fishes Biochem. J. 1979, 183, 317-323
    • (1979) Biochem. J. , vol.183 , pp. 317-323
    • Yancey, P.H.1    Somero, G.N.2
  • 11
    • 0038311869 scopus 로고    scopus 로고
    • Protein Stability in Mixed Solvents: A Balance of Contact Interaction and Excluded Volume
    • Schellman, J. A. Protein Stability in Mixed Solvents: A Balance of Contact Interaction and Excluded Volume Biophys. J. 2003, 85, 108-125
    • (2003) Biophys. J. , vol.85 , pp. 108-125
    • Schellman, J.A.1
  • 12
    • 0013789790 scopus 로고
    • Discussion of Human CO-hemoglobin by Urea, Guanidine Hydrochloride, and Other Reagents
    • Kawahara, K.; Kirshner, A. G.; Tanford, C. Discussion of Human CO-hemoglobin by Urea, Guanidine Hydrochloride, and Other Reagents Biochemistry 1965, 4, 1203-1213
    • (1965) Biochemistry , vol.4 , pp. 1203-1213
    • Kawahara, K.1    Kirshner, A.G.2    Tanford, C.3
  • 13
    • 0029081273 scopus 로고
    • Ginsburg, Urea-Induced Dissociation and Unfolding of Dodecameric Glutamine Synthetase from Escherichia Coli: Calorimetric and Spectral Studies
    • Zolkiewski, M.; Nosworthy, N.J. A. Ginsburg, Urea-Induced Dissociation and Unfolding of Dodecameric Glutamine Synthetase from Escherichia Coli: Calorimetric and Spectral Studies Protein Sci. 1995, 4, 1544-1552
    • (1995) Protein Sci. , vol.4 , pp. 1544-1552
    • Zolkiewski, M.1    Nosworthy, N.J.A.2
  • 14
    • 0016767776 scopus 로고
    • The Soybean Trypsin Inhibitor (Kunitz) is A Doubleheaded Inhibitor
    • Quast, U.; Steffen, E. The Soybean Trypsin Inhibitor (Kunitz) is A Doubleheaded Inhibitor Hoppe Seylers Z. Physiol. Chem. 1975, 356, 617-620
    • (1975) Hoppe Seylers Z. Physiol. Chem. , vol.356 , pp. 617-620
    • Quast, U.1    Steffen, E.2
  • 15
    • 26844533680 scopus 로고    scopus 로고
    • Composition Gradient Static Light Scattering: A New Technique for Rapid Detection and Quantitative Characterization of Reversible Macromolecular Hetero-Associations in Solution
    • Attri, A. K.; Minton, A. P. Composition Gradient Static Light Scattering: A New Technique for Rapid Detection and Quantitative Characterization of Reversible Macromolecular Hetero-Associations in Solution Anal. Biochem. 2005, 346, 132-138
    • (2005) Anal. Biochem. , vol.346 , pp. 132-138
    • Attri, A.K.1    Minton, A.P.2
  • 16
    • 58249085344 scopus 로고    scopus 로고
    • Fluorescence approaches to quantifying biomolecular interactions
    • Royer, C. A.; Scarlata, S. F. Fluorescence approaches to quantifying biomolecular interactions Methods Enzymol. 2008, 450, 79-106
    • (2008) Methods Enzymol. , vol.450 , pp. 79-106
    • Royer, C.A.1    Scarlata, S.F.2
  • 17
    • 0014143995 scopus 로고
    • Dimerization and Activity of Chymotrypsin at pH4
    • Morimoto, K.; Kegeles, G. Dimerization and Activity of Chymotrypsin at pH4 Biochemistry 1967, 6, 3007-3010
    • (1967) Biochemistry , vol.6 , pp. 3007-3010
    • Morimoto, K.1    Kegeles, G.2
  • 18
    • 0000800922 scopus 로고
    • Studies of Soybean Trypsin Inhibitor. I. Physicochemical Properties
    • Wu, Y. V.; Scheraga, H. A. Studies of Soybean Trypsin Inhibitor. I. Physicochemical Properties Biochemistry 1962, 1, 698-705
    • (1962) Biochemistry , vol.1 , pp. 698-705
    • Wu, Y.V.1    Scheraga, H.A.2
  • 20
    • 0015242084 scopus 로고
    • Dimerization of Alpha-Chymotrypsin. I. pH Dependence in the Acid Region
    • Aune, K. C.; Timasheff, S. N. Dimerization of Alpha-Chymotrypsin. I. pH Dependence in the Acid Region Biochemistry 1971, 10, 1609-1617
    • (1971) Biochemistry , vol.10 , pp. 1609-1617
    • Aune, K.C.1    Timasheff, S.N.2
  • 21
    • 0019880158 scopus 로고
    • Soybean Trypsin Inhibitor (Kunitz) is Doubleheaded. Kinetics of the Interaction of Alpha-Chymotrypsin with Each Side
    • Bosterling, B.; Quast, U. Soybean Trypsin Inhibitor (Kunitz) is Doubleheaded. Kinetics of the Interaction of Alpha-Chymotrypsin with Each Side Biochim. Biophys. Acta 1981, 657, 58-72
    • (1981) Biochim. Biophys. Acta , vol.657 , pp. 58-72
    • Bosterling, B.1    Quast, U.2
  • 22
    • 33645984885 scopus 로고    scopus 로고
    • Rapid Quantitative Characterization of Protein Interactions by Composition Gradient Static Light Scattering
    • Kameyama, K.; Minton, A. P. Rapid Quantitative Characterization of Protein Interactions by Composition Gradient Static Light Scattering Biophys. J. 2006, 90, 2164-2169
    • (2006) Biophys. J. , vol.90 , pp. 2164-2169
    • Kameyama, K.1    Minton, A.P.2
  • 25
    • 72249104136 scopus 로고    scopus 로고
    • Counteraction of Urea by Trimethylamine N-Oxide is Due to Direct Interaction
    • Meersman, F.; Bowron, D.; Soper, A. K.; Kock, M. H. Counteraction of Urea by Trimethylamine N-Oxide is Due to Direct Interaction Biophys. J. 2009, 97, 2559-2566
    • (2009) Biophys. J. , vol.97 , pp. 2559-2566
    • Meersman, F.1    Bowron, D.2    Soper, A.K.3    Kock, M.H.4
  • 26
    • 84857393452 scopus 로고    scopus 로고
    • Volume Exclusion and H-Bonding Dominate the Thermodynamics and Solvation of Trimethylamine-N-Oxide in Aqueous Urea
    • Rosgen, J.; Jackson-Atogi, R. Volume Exclusion and H-Bonding Dominate the Thermodynamics and Solvation of Trimethylamine-N-Oxide in Aqueous Urea J. Am. Chem. Soc. 2012, 134, 3590-3597
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 3590-3597
    • Rosgen, J.1    Jackson-Atogi, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.