Article
A nuclear magnetic resonance-based structural rationale for contrasting stoichiometry and ligand binding site(s) in fatty acid-binding proteins.
Biochemistry - 1 Mar 2011
He Yan, Estephan Rima, Yang Xiaomin, Vela Adriana, Wang Hsin, Bernard Cédric, Stark Ruth E
Abstract excerpt
Liver fatty acid-binding protein (LFABP) is a 14 kDa cytosolic polypeptide, differing from other family members in the number of ligand binding sites, the diversity of bound ligands, and the transfer of fatty acid(s) to membranes primarily via aqueous diffusion rather than direct collisional interactions. Distinct two-dimensional (1)H-(15)N nuclear magnetic resonance (NMR) signals indicative of slowly exchanging...
Topics
- Animals
- Binding Sites
- Fatty Acid-Binding Proteins
- Ligands
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- Nuclear Magnetic Resonance, Biomolecular
- Oleic Acid
- Protein Binding
- Protein Conformation
- Rats
- Static Electricity