Structure and mechanics of membrane proteins.
Evolution has tuned membrane proteins to exist in a lipid bilayer, provide for cell-cell communication, transport solutes, and convert energies. These proteins exhibit a hydrophobic belt that interacts with the lipid bilayer. Detergents are therefore used to extract membrane proteins and keep them in solution for purification and subsequent analyses. However, most membrane proteins are unstable when solubilized and hence often not accessible to NMR or X-ray crystallography. The atomic force microscope (AFM) is a powerful tool for imaging and manipulating membrane proteins in their native state. Superb images of native membranes have been recorded, and a quantitative interpretation of the data acquired using the AFM tip has become possible. In addition, multifunctional probes to simultaneously acquire information on the topography and electrical properties of membrane proteins have been produced. This progress is discussed here and fosters expectations for future developments and applications of AFM and single-molecule force spectroscopy.
Engel
Andreas
A
Maurice E. Müller Institute for Structural Biology, Biozentrum, University of Basel, Basel, Switzerland. andreas.engel@unibas.ch
Gaub
Hermann E
HE
D001105:Archaea / Q000378:metabolism*; D001436:Bacteriorhodopsins / Q000737:chemistry; D001671:Biochemistry / Q000379:methods*; D003460:Crystallization; D018360:Crystallography, X-Ray; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D008565:Membrane Proteins / Q000737:chemistry*; D018625:Microscopy, Atomic Force / Q000379:methods; D008928:Mitochondria / Q000378:metabolism; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D018717:Purple Membrane / Q000737:chemistry
D008024:Ligands; D008565:Membrane Proteins; D010455:Peptides; D001436:Bacteriorhodopsins