MAS NMR on a uniformly [13C, 15N] labeled LH2 light-harvesting complex from Rhodopseudomonas acidophila 10050 at ultra-high magnetic fields

Abstract

Solid State Nuclear Magnetic resonance (SSNMR) spectroscopy is considered to be one of the tools for structure determinations of membrane proteins, and this technique, along with X-ray crystallography, will play an important role in structural genomics projects. The goal of structural genomics is the determination of the 3-D structure of all human proteins or of the complete sets of proteins in particular functional classes, such as enzymes or cell-surface receptors. As of today, 19 different structures of polytopic membrane proteins from inner membranes of bacteria and mitochondria and from eukaryotic membranes, 16 structures of membrane proteins from the outer membrane of gram negative bacteria and related membrane proteins, and 4 structures of the monotopic membrane proteins that are only inserted into the membrane have been determined by crystallographic methods [1]. At the same time, about 2000 structures of water soluble proteins have been determined. SS NMR is a tool for structure determination of the membrane proteins that can not be crystallized and for the structure-functional studies of the membrane proteins of known structure. Within this context it is important to get assignment data for solid state NMR studies.