Article
Dominant role of local dipolar interactions in phosphate binding to a receptor cleft with an electronegative charge surface: equilibrium, kinetic, and crystallographic studies.
Protein science : a publication of the Protein Society - 1 Dec 1998
Ledvina P S, Tsai A L, Wang Z, Koehl E, Quiocho F A
Abstract excerpt
Stringent specificity and complementarity between the receptor, a periplasmic phosphate-binding protein (PBP) with a two-domain structure, and the completely buried and dehydrated phosphate are achieved by hydrogen bonding or dipolar interactions. We recently found that the surface charge potenti...
Topics
- Binding Sites
- Carrier Proteins
- Crystallography, X-Ray
- Fluorescence
- Kinetics
- Models, Molecular
- Mutation
- Osmolar Concentration
- Phosphate-Binding Proteins
- Phosphates
- Protein Conformation
- Recombinant Proteins
- Surface Properties
- Tryptophan