Regensburg 2010 – wissenschaftliches Programm
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CPP: Fachverband Chemische Physik und Polymerphysik
CPP 28: Poster: Biopolymers and Biomaterials
CPP 28.7: Poster
Mittwoch, 24. März 2010, 17:30–19:00, Poster C
Structure and Dynamics of the Myristoyl Lipid Modification of a Src Peptide Determined by 2H Solid-State NMR Spectroscopy — •Holger A. Scheidt1,2 and Daniel Huster1 — 1Institut für Medizinische Physik und Biophysik, Universität Leipzig, Leipzig, Deutschland — 2Institut für Biochemie/Biotechnologie, Martin-Luther-Universität Halle-Wittenberg, Halle, D
Lipid modifications of proteins are widespread in nature and play an important role in numerous biological processes. The nonreceptor tyrosine kinase Src is equipped with an N-terminal myristoyl chain and a cluster of basic amino acids for the stable membrane association of the protein. We used 2H NMR spectroscopy to investigate the structure and dynamics of the myristoyl chain of myr-Src(2-19) and compare them with the hydrocarbon chains of the surrounding phospholipids in bilayers of varying surface potential and chain length. The myristoyl chain of Src is well inserted in all bilayers investigated. In zwitterionic DMPC membranes, the myristoyl chain of Src is significantly longer and appears 'stiffer' than the phospholipid chains. This is explained by an equilibrium between the attraction due to the insertion of the myristoyl chain and the Born repulsion. In a DMPC/DMPS membrane, where attractive electrostatic interactions come into play, the differences between the peptide and the phospholipid chain lengths are attenuated and the molecular dynamics of all lipid chains is similar. In a much thicker DPPC/DPPS/cholesterol membrane, the length of the myristoyl chain of Src is elongated nearly to its maximum and their order parameters are comparable to those of the surrounding membrane.