Standard state and thermodynamic self-consistency

Journal of Pharmaceutical Sciences

Volumn 90, Issue 12, 2001, Pages 2099-2102

  Yu, Y Bruce ^a  

^a UNIVERSITY OF UTAH   (United States)

Author keywords

Biomacromolecules; Cratic entropy; Ideal mixing entropy; Standard state; Thermodynamic self consistency; Volumetric constraint

Indexed keywords

ARTICLE; DRUG SOLUBILITY; ENTROPY; MATHEMATICAL ANALYSIS; MOLECULAR DYNAMICS; STEADY STATE; THERMODYNAMICS; VALIDATION PROCESS;

EID: 0035213842     PISSN: 00223549     EISSN: None     Source Type: Journal    
DOI: 10.1002/jps.1160     Document Type: Article

References (19)

1. Specific volumes of biological macromolecules and some other molecules of biological interest
2. Partial molar volumes of polypeptides and their constituent groups in aqueous solution over a broad temperature range
3. Some factors in the interpretation of protein denaturation
4. Binding energy, specificity and enzyme catalysis: The circe effect
5. On the attribution of binding energy in antigen-antibody complexes McPC 603, D1.3, and HyHEL-5
6. Entropy in biological binding processes: Estimation of translational entropy loss
7. For Guldberg and Waage, with love and cratic entropy
8. The price of lost freedom
9. The development of a simple empirical scoring function to estimate the binding constant for a protein-ligand complex of known three-dimensional structure
10. The entropy cost of protein association
11. Contribution of translational and rotational entropy to the unfolding of a dimeric coiledcoil
12. Contribution of translational and rotational motions to molecular association in aqueous solution
13. The "cratic correction" and related fallacies
14. The statistical-thermodynamic basis for computation of binding affinities: A critical review
15. Loss of translational entropy in binding, folding, and catalysis
16. Comments on the comments