tailieunhanh - Báo cáo y học: "Protein-lipid interactions: correlation of a predictive algorithm for lipid-binding sites with three-dimensional structural data"

Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học quốc tế cung cấp cho các bạn kiến thức về ngành y đề tài: Protein-lipid interactions: correlation of a predictive algorithm for lipid-binding sites with three-dimensional structural data | Theoretical Biology and Medical Modelling BioMed Central Review Open Access Protein-lipid interactions correlation of a predictive algorithm for lipid-binding sites with three-dimensional structural data David L Scott 1 Gerold Diez2 and Wolfgang H Goldmann 1 2 Address 1Renal Unit Leukocyte Biology Inflammation Program Structural Biology Program and the Massachusetts General Hospital Harvard Medical School 149 13th Street Charlestown MA 02129 USA and 2Friedrich-Alexander-University of Erlangen-Nuremberg Center for Medical Physics and Technology Biophysics Group Henkestrasse 91 91052 Erlangen Germany Email David L Scott - dscott1@ Gerold Diez - gdiez@ Wolfgang H Goldmann - wgoldmann@ Corresponding authors Published 28 March 2006 Received 21 November 2005 Theoretical Biology and Medical Modelling 2006 3 17 doi 1742-4682-3-17 Accepted 28 March 2006 This article is available from http content 3 1 17 2006 Scott et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. 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 .