Molecular recognition between membrane-spanning polypeptides.
Integral membrane proteins have recently been shown to recognize and interact with other proteins within the membrane, either mimicking or altering their function, and with the lipid bilayer itself, resulting in a reorganization of native membrane protein. Membrane proteins are difficult to study using conventional methods such as X-ray crystallography, and so both synthesized and naturally occurring segments of membrane proteins have been used in the assessment of the mechanisms involved in their structure and organization.
Shai
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Department of Membrane Research and Biophysics, Weismann Institute of Science, Rehovot, Israel.
D000900:Anti-Bacterial Agents / Q000737:chemistry; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism*; D005397:Fish Venoms / Q000737:chemistry / Q000378:metabolism; D008563:Membrane Lipids / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D010455:Peptides; D010539:Permeability; D018272:Porins / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D012995:Solubility; D014763:Viral Matrix Proteins / Q000737:chemistry / Q000378:metabolism
D000900:Anti-Bacterial Agents; D005397:Fish Venoms; D008563:Membrane Lipids; D008565:Membrane Proteins; D010455:Peptides; D018272:Porins; D014763:Viral Matrix Proteins; C017603:pardaxin