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Volumn 118, Issue 47, 1996, Pages 11695-11700

On protein denaturation in aqueous-organic mixtures but not in pure organic solvents

Author keywords

[No Author keywords available]

Indexed keywords

LYSOZYME;

EID: 0029902287     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja961869d     Document Type: Article
Times cited : (379)

References (54)
  • 1
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    • Worth: New York, Our comments should not be construed as a criticism of this excellent textbook
    • Lehninger, A. L.; Nelson, D. L.; Cox, M. M. Principles of Biochemistry, 2nd ed.; Worth: New York, 1993; p 180. Our comments should not be construed as a criticism of this excellent textbook.
    • (1993) Principles of Biochemistry, 2nd Ed. , pp. 180
    • Lehninger, A.L.1    Nelson, D.L.2    Cox, M.M.3
  • 24
    • 0028304966 scopus 로고
    • Including X-ray crystallographic studies in anhydrous acetonitrile: Fitzpatrick, P. A.; Steinmetz, A. C. U.; Ringe, D.; Klibanov, A. M. Proc. Natl. Acad. Sci. U.S.A. 1993, 90, 8653-8657. Fitzpatrick, P. A.; Ringe D.; Klibanov, A. M. Biochem. Biophys. Res. Commun, 1994, 198, 675-681.
    • (1994) Biochem. Biophys. Res. Commun , vol.198 , pp. 675-681
    • Fitzpatrick, P.A.1    Ringe, D.2    Klibanov, A.M.3
  • 25
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    • note
    • 13 However, the extent of lysozyme denaturation in acetonitrile-water mixtures is pH-dependent and less pronounced for lysozyme obtained at neutral pH values. We chose pH 1.9 in this work to demonstrate the effect of protein denaturation at different acetonitrile concentrations in water most clearly.
  • 27
    • 10544238614 scopus 로고    scopus 로고
    • note
    • Using the amide III band spectral region. Solvent subtraction in the amide I region proved to be impossible at this acetonitrile concentration.
  • 29
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    • Reference 3
    • Chin et al. Reference 3.
    • Chin1
  • 31
    • 0016022523 scopus 로고
    • Because water, due to its ability to form multiple hydrogen bonds including those with proteins, acts as a molecular lubricant in protein systems: Kuntz, I. D.; Kauzmann. W. Adv. Protein Chem. 1974, 28, 239-245. Finney, J. L.; Poole, P. L. Comments Mol. Cell. Biophys. 1984, 2, 129-151. Rupley, J. A.; Careri, G. Adv. Protein Chem. 1991, 41, 37-172. Gregory, R. B., Ed. Protein-Solvent Interactions; M. Dekker: New York, 1995.
    • (1974) Adv. Protein Chem. , vol.28 , pp. 239-245
    • Kuntz, I.D.1    Kauzmann, W.2
  • 32
    • 0016022523 scopus 로고
    • Because water, due to its ability to form multiple hydrogen bonds including those with proteins, acts as a molecular lubricant in protein systems: Kuntz, I. D.; Kauzmann. W. Adv. Protein Chem. 1974, 28, 239-245. Finney, J. L.; Poole, P. L. Comments Mol. Cell. Biophys. 1984, 2, 129-151. Rupley, J. A.; Careri, G. Adv. Protein Chem. 1991, 41, 37-172. Gregory, R. B., Ed. Protein-Solvent Interactions; M. Dekker: New York, 1995.
    • (1984) Comments Mol. Cell. Biophys. , vol.2 , pp. 129-151
    • Finney, J.L.1    Poole, P.L.2
  • 33
    • 0025877453 scopus 로고
    • Because water, due to its ability to form multiple hydrogen bonds including those with proteins, acts as a molecular lubricant in protein systems: Kuntz, I. D.; Kauzmann. W. Adv. Protein Chem. 1974, 28, 239-245. Finney, J. L.; Poole, P. L. Comments Mol. Cell. Biophys. 1984, 2, 129-151. Rupley, J. A.; Careri, G. Adv. Protein Chem. 1991, 41, 37-172. Gregory, R. B., Ed. Protein-Solvent Interactions; M. Dekker: New York, 1995.
    • (1991) Adv. Protein Chem. , vol.41 , pp. 37-172
    • Rupley, J.A.1    Careri, G.2
  • 34
    • 0016022523 scopus 로고
    • M. Dekker: New York
    • Because water, due to its ability to form multiple hydrogen bonds including those with proteins, acts as a molecular lubricant in protein systems: Kuntz, I. D.; Kauzmann. W. Adv. Protein Chem. 1974, 28, 239-245. Finney, J. L.; Poole, P. L. Comments Mol. Cell. Biophys. 1984, 2, 129-151. Rupley, J. A.; Careri, G. Adv. Protein Chem. 1991, 41, 37-172. Gregory, R. B., Ed. Protein-Solvent Interactions; M. Dekker: New York, 1995.
    • (1995) Protein-Solvent Interactions
    • Gregory, R.B.1
  • 51
    • 0024101334 scopus 로고
    • -1 was 34 ± 0%, i.e., in agreement with the X-ray structural data. Analysis of the IR spectrum in the amide III spectral region afforded a similar α-helix content of 30 ± 1%, thereby further verifying the band assignment in the amide I region.
    • (1988) Protein Eng. , vol.2 , pp. 271-276
    • Neidhart, D.J.1    Petsko, G.A.2
  • 54
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    • note
    • The solubility of subtilisin in organic solvents is below that of lysozyme. While lysozyme in 60% acetonitrile is still in solution at 50 mg/ mL, subtilisin is not completely soluble under these conditions.


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