Partial Molar Isentropic Compressions of Some Tetra- and Pentapeptides in Aqueous Solution: Implications for Group Additivity Schemes for Unfolded Proteins
Author:
Publisher
Springer Science and Business Media LLC
Subject
Physical and Theoretical Chemistry,Molecular Biology,Biochemistry,Biophysics
Link
http://link.springer.com/content/pdf/10.1007/s10953-012-9818-3.pdf
Reference42 articles.
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3. Ohmae, E., Murakami, C., Gekko, K., Kato, C.: Pressure effects on enzyme functions. J. Biol. Macromol. 7, 23–29 (2007)
4. Heremans, K., Smeller, L.: In: Taniguchi, Y., Stanley, H.E., Ludwig, H. (eds.) Biological Systems Under Extreme Conditions: Structure and Function, p. 53. Springer, Berlin (2002)
5. Chalikian, T.V.: Volumetric properties of proteins. Annu. Rev. Biophys. Biomol. Struct. 32, 207–235 (2003)
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1. Volumetric Properties at High Pressures of the Nucleosides Inosine, 2′-Deoxyinosine, and 2′-Deoxyguanosine and the Volumetric Properties of Guanosine Derived Using Group Additivity Methods;Journal of Chemical & Engineering Data;2014-09-22
2. Volumetric Properties of the Nucleoside Thymidine in Aqueous Solution at T = 298.15 K and p = (10 to 100) MPa;Journal of Solution Chemistry;2014-04
3. Group-contribution to limiting partial molar isentropic compressions of small amphiphile molecules in water. The temperature effect;The Journal of Chemical Thermodynamics;2014-02
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