Aspects of weak interactions
- 1 January 1998
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Chemical Society Reviews
- Vol. 27 (1) , 57-64
- https://doi.org/10.1039/a827057z
Abstract
Weak interactions, such as those non-covalent interactions that occur in biological systems, are less well characterised than their strong, covalent counterparts. Here, we discuss associations between two or more molecules and consider the effect of interactions with solvent molecules (particularly water) and changes in the internal structure of the associating molecules on binding. We go on to discuss some of the progress that has been made in the estimation of binding constants.Keywords
This publication has 35 references indexed in Scilit:
- Successful Predictions of the Residual Motion of Weakly Associated Species as a Function of the Bonding between ThemThe Journal of Physical Chemistry, 1996
- Win some, lose some: enthalpy-entropy compensation in weak intermolecular interactionsChemistry & Biology, 1995
- Application of a generalised enthalpy–entropy relationship to binding co-operativity and weak associations in solutionJournal of the Chemical Society, Perkin Transactions 2, 1995
- The cost of conformational order: entropy changes in molecular associationsJournal of the American Chemical Society, 1992
- Effect of alanine versus glycine in α-helices on protein stabilityNature, 1992
- Extracting hydrophobic free energies from experimental data: relationship to protein folding and theoretical modelsBiochemistry, 1991
- The hydrogen bond in molecular recognitionTrends in Biochemical Sciences, 1987
- Temperature dependence of the hydrophobic interaction in protein folding.Proceedings of the National Academy of Sciences, 1986
- Hydrogen bonding and biological specificity analysed by protein engineeringNature, 1985
- On the attribution and additivity of binding energiesProceedings of the National Academy of Sciences, 1981