Molecular and biological constraints on ligand-binding affinity and specificity
- 1 January 1997
- journal article
- review article
- Published by Wiley in Biopolymers
- Vol. 44 (2), 181-198
- https://doi.org/10.1002/(sici)1097-0282(1997)44:2<181::aid-bip5>3.0.co;2-r
Abstract
Interactions between biological macromolecules have characteristic values of affinity and specificity that are set according to the biological function that is served by the interaction in the organism. Here we examine the molecular mechanisms that are used to achieve the required values of affinity and specificity in various biological systems.Keywords
This publication has 79 references indexed in Scilit:
- How Proteins Recognize the TATA BoxJournal of Molecular Biology, 1996
- Global Changes in Amide Hydrogen Exchange Rates for a Protein Antigen in Complex with Three Different AntibodiesJournal of Molecular Biology, 1996
- Decomposition of the Free Energy of a System in Terms of Specific InteractionsJournal of Molecular Biology, 1994
- The Solution Structures of the trp Repressor-Operator DNA ComplexJournal of Molecular Biology, 1994
- Local and Transmitted Conformational Changes on Complexation of an Anti-sweetener FabJournal of Molecular Biology, 1994
- Crystal structure of a yeast TBP/TATA-box complexNature, 1993
- Refined Solution Structures of the Escherichia coli trp Holo- and AporepressorJournal of Molecular Biology, 1993
- Refined crystal structure of the influenza virus N9 neuraminidase-NC41 Fab complexJournal of Molecular Biology, 1992
- Crystals of the complex between human growth hormone and the extracellular domain of its receptorJournal of Molecular Biology, 1991
- Ordered water structure around a B-DNA dodecamerJournal of Molecular Biology, 1983