Protein-lipid interactions: correlation of a predictive algorithm for lipid-binding sites with three-dimensional structural data.

ABSTRACT:

Background

Over the past decade our laboratory has focused on understanding how soluble cytoskeleton-associated proteins interact with membranes and other lipid aggregates. Many protein domains mediating specific cell membrane interactions appear by fluorescence microscopy and other precision techniques to be partially inserted into the lipid bilayer. It is unclear whether these protein-lipid-interactions are dependent on shared protein motifs or unique regional physiochemistry, or are due to more global characteristics of the protein.

Results

We have developed a novel computational program that predicts a protein's lipid-binding site(s) from primary sequence data. Hydrophobic labeling, Fourier transform infrared spectroscopy (FTIR), film balance, T-jump, CD spectroscopy and

SUBMITTER: Scott DL 

PROVIDER: S-EPMC1523333 | biostudies-literature | 2006 Mar

REPOSITORIES: biostudies-literature