Martin Rademacher

TL;DR: The features of E-FABP backbone dynamics elaborated in the present study differ markedly from those of the phylogenetically closely related heart-type FABP and the more distantly related ileal lipid-binding protein, implying a strong interdependence with the overall protein stability and possibly also with the ligand-binding affinity for members of the lipid- binding protein family.

TL;DR: Although apoCRBP contains a binding cavity more shielded than that of any other retinoid carrier, conformational flexibility in the portal region may assist retinol uptake, and the stiffening of the backbone in the holoprotein guarantees the stability of the complex during ret inol transport and suggests that targeted retinols release requires a transiently open state that is likely to be promoted by the acceptor or the local environment.

TL;DR: The three-dimensional solution structure of human heart-type FABP is determined by multi-dimensional heteronuclear NMR spectroscopy and shows that different fatty acids induce distinct conformational states of the protein backbone in this portal region, depending on the chain length of the fatty acid ligand.

TL;DR: The magnetic relaxation dispersion of the water 17O resonance is used to investigate the water molecules in the binding cavity of three different lipid-binding proteins and finds that ligand binding actually increases the number of water molecules within the cavity.

TL;DR: Comparison with data from other LBPs implies that the evolutionary specialization of LBPs for certain ligand types was not only because of mutations of residues directly involved in ligand binding but also to a refinement of the internal water scaffold.