Robert Feulgen Lecture. Microscopic assessment of membrane protein structure and function.
Membrane proteins represent an important class of proteins that are encoded by about 40% of all genes, but compared to soluble proteins structural information is sparse. Most of the atomic coordinates currently available are from bacterial membrane proteins and have been obtained by X-ray crystallography. Recent results demonstrate the imaging power of the atomic force microscope and the accuracy of electron crystallography. These methods allow membrane proteins to be studied while embedded in the bilayer, and thus in a functional state. The low signal-to-noise ratio of cryoelectron microscopy is overcome by crystallizing membrane proteins in a two-dimensional protein-lipid membrane, allowing its atomic structure to be determined. In contrast, the high signal-to-noise ratio of atomic force microscopy allows individual protein surfaces to be imaged at subnanometer resolution, and their conformational states to be sampled. This review discusses examples of microscopic membrane protein structure determination and illuminates recent progress.
Engel
Andreas
A
M.E. Müller Institute for Microscopy, Biozentrum, University of Basel, Klingelbergstrasse 70, 4056 Basel, Switzerland. andreas.engel@unibas.ch
D000818:Animals; D020346:Aquaporins / Q000502:physiology / Q000648:ultrastructure; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000502:physiology / Q000648:ultrastructure; D008565:Membrane Proteins / Q000737:chemistry* / Q000502:physiology / Q000648:ultrastructure*; D018625:Microscopy, Atomic Force; D018272:Porins / Q000502:physiology / Q000648:ultrastructure; D012243:Rhodopsin / Q000502:physiology / Q000648:ultrastructure
D020346:Aquaporins; D001425:Bacterial Outer Membrane Proteins; D008565:Membrane Proteins; D018272:Porins; D012243:Rhodopsin