Weak interactions and lessons from crystallization

Chemistry and Biology

Volumn 3, Issue 9, 1996, Pages 695-701

  Williams, Dudley H ^a   Westwell, Martin S ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0030250593     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(96)90243-4     Document Type: Article

References (26)

1. Pauling, L. (1946). Molecular architecture and biological reactions. Chem. Eng. News 24, 1375-1377.
2. Gavezzotti, A. (1994). Are crystal structures predictable? Accounts Chem. Res. 27, 309-314.
3. Williams, D.H. & Westwell, M.S. (1996). Aspects of weak interactions. Accounts Chem. Res., in press.
4. Westwell, M.S., Searle, M.S., Wales, D.J. & Williams, D.H. (1995). Empirical correlations between thermodynamic properties and intermolecular forces. J. Am. Chem. Soc. 117, 5013-5015.
5. Westwell, M.S., Searle, M.S. & Williams, D.H. (1996). The 'n' effect in biological molecular recognition. J. Mol. Recogn., in press.
6. Hill, T.L. (1963). Thermodynamics of Small Systems. Part 1. Benjamin, New York.
7. Dasent, W.E. (1982). Inorganic Energetics - An Introduction. Cambridge University Press, Cambridge.
8. Porschke, D. (1971). Cooperative nonenzymatic base recognition II. Thermodynamics of the helix-coil transition of oligoadenylic + oligouridylic acids. Biopolymers 10, 1989-2013.
9. Morrison, J.A., Drain, L.E. & Dugdale, J.S. (1952). Phase transitions in multimolecular layers of adsorbed nitrogen. Can. J. Chem. 30, 890-903.
10. Mackay, J.P., Gerhard, U., Beauregard, D.A., Westwell, M.S., Searle, M.S. & Williams, D.H. (1994). Glycopeptide antibiotic activity and the possible role of dimerization: a model for biological signalling. J. Am. Chem. Soc. 116, 4581-4590.
11. Batta, G., Cristofaro, M.F., Sharman, G.J. & Williams, D.H. (1996). Demonstration of the difference in binding affinity between the two binding sites of the ristocetin A asymmetric dimer. J. Chem. Soc., Chem. Commun. 101-103.
12. Beauregard, D.A., Williams, D.H., Gwynn, M.N. & Knowles, D.J. (1995). Dimerization and membrane anchors in extracellular targeting of vancomycin group antibiotics. Antimicrob. Agents Chemother. 39, 781-785.
13. Ladbury, J.E., Wright, J.G., Sturtevant, J.M. & Sigler, P.B. (1994). A thermodynamic study of the trp repressor-operator interaction. J. Mol. Biol. 238, 669-681.
14. Green, N.M. (1975). Avidin. Adv. Protein Chem. 29, 85-133.
15. Sano, T. & Cantor, C.R. (1995). Intersubunit contacts made by tryptophan 120 with biotin are essential for both strong biotin binding and biotin-induced tighter subunit association of streptavidin. Proc. Natl. Acad. Sci. USA 92, 3180-3184.
16. Jones, M.L. & Kurzban, G.P. (1995). Noncooperativity of biotin binding to tetrameric streptavidin. Biochemistry 34, 11750-11756.
17. Perutz, M.F. (1978). Haemoglobin structure and respiratory transport. Sci. Am. 239, 92-123.
18. Perutz, M.F. (1970). Stereochemistry of cooperative effects in haemoglobin. Nature 228, 726-734.
19. Weber, P.C., Wendoloski, J.J., Pantoliano, M.W. & Salemme, F.R. (1992). Crystallographic and thermodynamic comparison of natural and synthetic ligands bound to streptavidin. J. Am. Chem. Soc. 114, 3197-3200.
20. 2 engineering. 6. Single amino-acid substitutions of active-site residues converts rigid enzyme to highly flexible conformational states. J. Am. Chem. Soc. 114, 2748-2749.
21. Wilde, J.A., Bolton, P.H., Dell'Acqua, M., Hibler, D.W., Pourmotabbed, T. & Gerlt, J.A. (1988). Identification of residues involved in a conformational change accompanying substitutions for glutamate-43 in staphylococcal nuclease. Biochemistry 27, 4127-4132.
22. Loll, P.J. & Lattman, E.E. (1990). Active-site mutant Glu43→Asp in staphylococcal nuclease displays nonlocal structural changes. Biochemistry 29, 6866-6873.
23. 2 studied in solution by NMR spectroscopy. Eur. J. Biochem. 211, 437-447.
24. Chen, C., Roberts, V.A., Stevens, S., Brown, M., Stenzel-Poore, M.P. & Rittenberg, M.B. (1995). Enhancement and destruction of antibody function by somatic mutation: unequal occurance is controlled by V gene combinatorial associations. EMBO J. 14, 2784-2794.
25. Patten, P.A., et al., & Schultz, P.G. (1996). The immunological evolution of catalysis. Science 271, 1086-1091.
26. Westwell, M.S., Bardsley, B., Dancer, R.J., Try, A.C. & Williams, D.H. (1996). Cooperativity in ligand binding expressed at a model cell membrane by the vancomycin group antibiotics. J.Chem. Soc., Chem. Commun., 589-590.