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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.
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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.
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10544255895
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note
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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.
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26
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0028875052
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Costantino, H. R.; Griebenow, K.; Mishra, P.; Langer, R.; Klibanov, A. M. Biochim. Biophys. Acta 1995, 1253, 69-74.
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10544238614
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note
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Using the amide III band spectral region. Solvent subtraction in the amide I region proved to be impossible at this acetonitrile concentration.
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29
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10544229524
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Reference 3
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Chin et al. Reference 3.
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Chin1
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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.
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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.
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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.
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M. Dekker: New York
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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.
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Peaks with similar frequencies were reported in the literature for second-derivative spectra of an aqueous solution of lysozyme at pH 7.4: Gorga, J. C.; Dong. A.; Manning, M. C.; Woody, R. W.; Caughey, W. S.; Strominger, J. L. Proc. Natl. Acad. Sci. U.S.A. 1989, 86, 2321-2325.
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0024101334
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-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.
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10544221820
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note
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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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