All-Purpose Containers? Lipid-Binding Protein – Drug Interactions

All-Purpose Containers? Lipid-Binding Protein – Drug Interactions

The combined use of in vitro (19F-NMR) and in silico (molecular docking) procedures demonstrates the affinity of a number of human calycins (lipid-binding proteins from ileum, liver, heart, adipose tissue and epidermis, and retinol-binding protein from intestine) for different drugs (mainly steroids and vastatins). Comparative evaluations on the complexes outline some of the features relevant f...

drug-protein interactions: binding of serotonin and arachidonyl serotonin to β-lactoglobulin

Inositol-lipid binding motifs: signal integrators through protein-lipid and protein-protein interactions.

Inositol lipids have emerged as universal lipid regulators of protein signaling complexes in defined membrane compartments. The number of protein modules that are known to recognise these membrane lipids is rapidly increasing. Pleckstrin homology domains, FYVE domains, PX domains, ENTH domains, CALM domains, PDZ domains, PTB domains and FERM domains are all inositide-recognition modules. The la...

Lipid-protein interactions.

Intrinsic membrane proteins are solvated by a shell of lipid molecules interacting with the membrane-penetrating surface of the protein; these lipid molecules are referred to as annular lipids. Lipid molecules are also found bound between transmembrane α-helices; these are referred to as non-annular lipids. Annular lipid binding constants depend on fatty acyl chain length, but the dependence is...

Protein-Lipid Interactions - ReadingSample

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