University of Minnesota research by Judith M. LaLonde examines the binding of adipocyte lipid-binding protein (ALBP) to arachidonic and oleic acids. The dataset includes thermodynamic parameters from isothermal titration calorimetry, such as dissociation constants (Kd) and enthalpy changes, and structural details from a 1.6 Å resolution crystal structure. These results provide a framework for understanding the molecular basis of protein-lipid interactions.
Use Cases
- Modeling protein-lipid binding affinities based on reported thermodynamic parameters like Kd and delta G.
- Analyzing ligand conformation within protein cavities based on the described hairpin structure of arachidonate.
- Comparing enthalpic and entropic contributions to binding for different unsaturated fatty acids.
- Validating computational docking simulations using the high-resolution (1.6 Å) crystal structure data.
Strengths
- Includes specific thermodynamic parameters: Kd = 4.4 microM for arachidonic acid and Kd = 2.4 microM for oleic acid.
- Crystallographic refinement was carried out to a high resolution of 1.6 Å with an R factor of 0.19.
- Identifies key protein residues (Arg106, Arg126, Tyr128) interacting with the fatty acid carboxylate.
Limitations
- Row count is unknown, which may limit suitability assessment.
- Column-level documentation is absent; field semantics must be inferred after download.
- Last update date is unknown; freshness unverified.
Provenance
- Source
- University of Minnesota, Judith M. LaLonde
- Collection Method
- Isothermal titration calorimetry and X-ray crystallography.