Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Thermodynamics proteins

Abstract. Walter Kauzmann stated in a review of protein thermodynamics that volume and enthalpy changes are equally fundamental properties of the unfolding process, and no model can be considered acceptable unless it accounts for the entire thermodynamic behaviour (Nature 325 763-764, 1987). While the thermodynamic basis for pressure effects has been known for some time, the molecular mechanisms have remained rather mysterious. We, and others in the rather small field of pressure effects on protein structure and stability, have attempted since that time to clarify the molecular and physical basis for the changes in volume that accompany protein conformational transitions, and hence to explain pressure effects on proteins. The combination of many years of work on a model system, staphylococcal nuclease and its large numbers of site-specific mutants, and the rather new pressure perturbation calorimetry approach has provided for the first time a fundamental qualitative understanding of AV of unfolding, the quantitative basis of which remains the goal of current work. [Pg.173]

Barratt, J.O., Thrombin and calcium chloride in relation to coagulation, Biochem. J. 9, 511-543, 1915 Van der Meer, C., Effect of calcium chloride on choline esterase. Nature 171, 78-79, 1952 Bhat, R. and Ahluwalia, J.C., Effect of calcium chloride on the conformation of proteins. Thermodynamic studies of some model compounds, Int. J. Pept. Protein Res. 30,145-152,1987 Furihata, C., Sudo, K., and Matsushima, T, Calcium chloride inhibits stimulation of replicative DNA... [Pg.263]

Protein Thermodynamics Protein Interactions Computational Protein Design Conclusions... [Pg.1624]

IV.2. Monte Carlo equilibrium simulations of ligand-protein thermodynamics... [Pg.306]

Sola, R.J., Al-Azzam, W., Griebenow, K. Engineering of protein thermodynamic, kinetic, and colloidal stability Chemical glycosylation with monofunctionally activated glycans. Biotechnol. Bioeng. 2006, 94,1072-9. [Pg.279]

Takagi, F., Koga, N., Takada, S. How protein thermodynamics and folding mechanisms are altered by the chaperonin cage Molecular simulations. Proc. Natl. Acad. Sci. U.S.A. 2003,100, 11367-72. [Pg.279]

The previously discussed models fall under the category of linkage models in that the protein species are all identified and linked together with the energies for their formation controlling their relative prevalence. These models work well as approximations but fall short for descriptions of true protein thermodynamics where multiple conformations of unknown identity can coexist. Linkage model approximations can be used to define the... [Pg.53]

Figure 2 Examples of free energy change variation as a function of temperature for some examples of globular proteins. (Thermodynamic data obtained by DSC.) ALA (pH 6.5) a-lactalbumin at pH 6.5. (Data from Ref. 190.) BLG (pH 2) /3-Iactoglobulin at pH 2. (Data from Ref. 28.) BLG (pH 3.5) /3-laetoglobulin at pH 3.5. (Data from Ref. 45.) BSA (pH 7) bovin serum albumin. (Data from Ref. 64.)... Figure 2 Examples of free energy change variation as a function of temperature for some examples of globular proteins. (Thermodynamic data obtained by DSC.) ALA (pH 6.5) a-lactalbumin at pH 6.5. (Data from Ref. 190.) BLG (pH 2) /3-Iactoglobulin at pH 2. (Data from Ref. 28.) BLG (pH 3.5) /3-laetoglobulin at pH 3.5. (Data from Ref. 45.) BSA (pH 7) bovin serum albumin. (Data from Ref. 64.)...
Damodaran, S. J.E. Kinsella. Interaction of carbonyls with soy protein thermodynamic effects./. Agric. Food Chem. 1981a, 29, 1249-1253. [Pg.264]

Metabolic pathways of microorganisms Portal to ProTherm (protein thermodynamics), ProNit (protein-nucleic acid interactions), biomolecule structures Crystal data and crystallization conditions for proteins, nucleic acids, and complexes Enzyme nomenclature and properties See B.5... [Pg.2538]

Portal to ProTherm (protein thermodynamics), ProNit (protein-nucleic acid interactions), biomolecule structures, etc. [Pg.2315]

The following review provides a basis for understanding the theoretical development used to eonstruct the model presented in this chapter. Emphasis is placed on basic protein biophysics and the importance of sohd surface hydrophobicity and protein thermodynamic stabiUty on adsorption. [Pg.804]

Celey, M.S. Dassie, S.A. Freire, E. Bianconi, M.L. Fideho, G.D. (2005) Ligand induced thermostability in proteins Thermodynamic analysis of ANS-albumin interaction. [Pg.294]

The decrease of protein thermodynamic stability on pH decreasing suggests a preferential binding of protons to the unfolded state. The effect of pH on the standard denaturation Gibbs function, tyfi, has been theoretically analyzed by... [Pg.905]


See other pages where Thermodynamics proteins is mentioned: [Pg.265]    [Pg.97]    [Pg.314]    [Pg.138]    [Pg.158]    [Pg.214]    [Pg.255]    [Pg.1627]    [Pg.118]    [Pg.22]    [Pg.79]    [Pg.310]    [Pg.274]   
See also in sourсe #XX -- [ Pg.200 ]




SEARCH



Basic Thermodynamics of Protein-Ligand Interactions

Cooperativity, protein folding thermodynamics

Experimental Approaches to Determine the Thermodynamics of Protein-Ligand Interactions

Globular proteins thermodynamic parameters

Ligand-protein Thermodynamics

Monte Carlo equilibrium simulations of ligand-protein thermodynamics

Protein carbohydrate thermodynamic data

Protein carbohydrate thermodynamics 1/887- conformation

Protein folding thermodynamic studies

Protein folding thermodynamics

Protein self assembly, thermodynamics

Protein stability thermodynamics

Protein structure thermodynamics

Proteins thermodynamic compatibility

Proteins thermodynamic incompatibility

Proteins thermodynamic quantities

Proteins thermodynamic stability

Proteins, ligand binding thermodynamics

The Thermodynamics of Protein-Carbohydrate Interaction

The thermodynamic stability hypothesis Protein results

Thermodynamic Analysis of Protein Structure Stability

Thermodynamic Studies of Protein Stabilities

Thermodynamic approach to protein denaturation

Thermodynamic hypothesis, of protein

Thermodynamic hypothesis, of protein folding

Thermodynamic lead-protein interactions

Thermodynamic properties Proteins

Thermodynamic protein results

Thermodynamic studies, proteins

Thermodynamics and kinetics of protein

Thermodynamics and kinetics of protein folding

Thermodynamics calculation from protein structure

Thermodynamics of protein adsorption

Thermodynamics of protein binding

Thermodynamics of protein folding

Thermodynamics of proteins

Thermodynamics protein binding

Thermodynamics protein folding/unfolding

Thermodynamics protein solutions

Thermodynamics protein-ligand interactions

Thermodynamics protein—salt-water interactions

Thermodynamics, water-protein

© 2024 chempedia.info