Probing Specific Lipid-Protein Interaction by Saturation Transfer Difference NMR Spectroscopy

摘要

Recently attention has focused again on the importance of the lipid matrix for function of integral membrane proteins.From early EPR and NMR studies it is well-known that lipids in a first layer surrounding integral membrane proteins have different dynamic properties.By fluorescence spectroscopy as well as chemical cross-linking,evidence for preferential interactions between particular lipid species and proteins was obtained.More recently,the existence of tightly bound lipids in membrane protein crystals was reported.While the importance of those observations is indisputable,such experiments should be conducted in the biologically relevant liquid crystalline state of the lipid matrix without using potentially perturbing labels.