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Tanford

Reynolds J A, Gilbert D B and Tanford C 1974 Empirieal eorrelation between hydrophobie free energy and aqueous eavity surfaee area Proc. Natl Acad. Sc/. USA 71 2925-7... [Pg.2604]

Tanford, C., Kirkwood, J. G. Theory of protein titration curves. I. General equations for impenetrable spheres. J. Am. Chem. Soc. 79 (1957) 5333-5339. 6. Garrett, A. J. M., Poladian, L. Refined derivation, exact solutions, and singular limits of the Poisson-Boltzmann equation. Ann. Phys. 188 (1988) 386-435. Sharp, K. A., Honig, B. Electrostatic interactions in macromolecules. Theory and applications. Ann. Rev. Biophys. Chem. 19 (1990) 301-332. [Pg.194]

Tanford, C., Roxby, R. Interpretation of protein titration curves Application to lysozyme. Biochem. 11 (1972) 2192-2198. [Pg.195]

How can Equation (11.79) be solved Before computers were available only simple ihapes could be considered. For example, proteins were modelled as spheres or ellipses Tanford-Kirkwood theory) DNA as a uniformly charged cylinder and membranes as planes (Gouy-Chapman theory). With computers, numerical approaches can be used to solve the Poisson-Boltzmann equation. A variety of numerical methods can be employed, including finite element and boundary element methods, but we will restrict our discussion to the finite difference method first introduced for proteins by Warwicker and Watson [Warwicker and Watson 1982]. Several groups have implemented this method here we concentrate on the work of Honig s group, whose DelPhi program has been widely used. [Pg.620]

Tanford, C.,PhysicalChemistry of Macromolecules, Ii ey,Ne N York, 1961. Tompa, H., Po/jgmer Butterworths, London, 1956. [Pg.582]

Tanford, C., Physical Chemistry of Macromolecules, Wiley, New York, 1961. [Pg.658]

The Stokes-Einstein equation has already been presented. It was noted that its vahdity was restricted to large solutes, such as spherical macromolecules and particles in a continuum solvent. The equation has also been found to predict accurately the diffusion coefficient of spherical latex particles and globular proteins. Corrections to Stokes-Einstein for molecules approximating spheroids is given by Tanford. Since solute-solute interactions are ignored in this theory, it applies in the dilute range only. [Pg.598]

C. Tanford. The Hydrophobic Effect Formation of Micelles and Biological Membranes. New York Wiley, 1980. [Pg.674]

Tanford. C. The Hydrophobic Effect", 2nd ed. Wiley-Interscience New York, 1980. [Pg.457]

Adapted from Cantor, C., and Schimmel, P., 1980. Biophysical Chemistry.. San Franci.sco W.H. Freeman, and Tanford, C., 1968. Protein denatnration. Advances in Protein Chemistry 23 121-282. [Pg.59]

Berry, R. S., Rice, S. A., and Ross, J., 1980. Physical Chemistry. New York John Wiley. Tanford, C., 1980. The Hydrojshobic Effect. New York John Wiley. [Pg.64]

However is not to measure solution density at each concentration since the correction of Tanford (1955) can be applied ... [Pg.96]

Tanford, Charles. The electrostatic free energy of globular protein ions in aqueous salt solution. Journal of Physical Chemistry 59 (1955) 788-793. [Pg.115]

Tanford, C. (1980). The Hydrophobic Effect (2nd edition). New York Wiley-lnterscience. [Pg.370]

Ueno, M., Tanford, C., and Reynolds, J. A. (1984). Phospholipid vesicle formation using nonionic detergents with low monomer solubility. Kinetic factors determine vesicle size and polydis-persity. Biochemistry, 3070-3076. [Pg.337]

The charge of a number of proteins has been measured by titration. The early experimental work focused on the determination of charge as a function of pH later work focused on comparing the experimental and theoretical results the latter obtained from the extensions of the Tanford-Kirkwood models on the electrostatic behavior of proteins. Ed-sall and Wyman [104] discuss the early work on the electrostatics of polar molecules and ions in solution, considering fundamental coulombic interactions and accounting for the dielectric properties of the media. Tanford [383,384], and Tanford and Kirkwood [387] describe the development of the Tanford-Kirkwood theories of protein electrostatics. For more recent work on protein electrostatics see Lenhoff and coworkers [64,146,334]. [Pg.588]

Shire, SJ Hanania, GIH Gurd, FRN, Electrostatic Effects in Myoglobin. Application of the Modified Tanford-Kirkwood Theory to Myoglobins from Elorse, California Grey Whale, Harbor Seal, and California Sea Lion, Biochemistry 14, 1352, 1975. [Pg.621]

Tanford, C, Theory of Protein Titration Curves. 11. Calculations for Simple Models at Low Ionic Strength, Journal of the American Chemical Society 79, 5340, 1957. [Pg.622]

Tanford, C Haueinstein, JD, Phenolic Hydroxyl Ionization in Proteins. II. Ribonuclease, Journal of the American Chemical Society 78, 5287, 1956. [Pg.622]

Tanford, C Roxy, Interpretation of Protein Titration Curves Application to Lysozyme, Biochemistry 11, 2192, 1972. [Pg.622]

Tanford, C Swanson, SA Shore, WS, Hydrogen Ion EquUihria of Bovine Serum Alhumin, Journal of the American Chemical Society 77, 6414, 1955. [Pg.622]

Tanford C. The hydrophobic effect formation of micelles and biological membranes. New York John Wiley Sons, 1980. [Pg.349]


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Tanford, Charles

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Tanford’s formulae

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