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In contrast, approximately 25% of all proteins are membrane proteins. [15] Their hydrophobic surfaces make structural and especially functional characterization difficult. [13] [16] Detergents can be used to render membrane proteins water-soluble, but these can also alter protein structure and function. [13]
Proteins structures are taken from the Protein Data Bank. OPM also provides structural classification of membrane-associated proteins into families and superfamilies, membrane topology, quaternary structure of proteins in membrane-bound state, and the type of a destination membrane for each protein. The coordinate files with calculated membrane ...
David Tudor Jones FRS (born 1966) [2] is a Professor of Bioinformatics, and Head of Bioinformatics Group in the University College London. [3] He is also the director in Bloomsbury Center for Bioinformatics, which is a joint Research Centre between UCL and Birkbeck, University of London and which also provides bioinformatics training and support services to biomedical researchers.
Carolyn Cohen — in 1969, Cohen codiscovered the molecular structure of tropomyosin as a polar coiled coil, also being the first protein crystal structure determined with a 20Å resolution via x-ray crystallography. On the route to this discovery, she also discovered a novel crystal structure, termed the Cohen-Longley paracrystal with 400Å ...
An integral, or intrinsic, membrane protein (IMP) [1] is a type of membrane protein that is permanently attached to the biological membrane. All transmembrane proteins can be classified as IMPs, but not all IMPs are transmembrane proteins. [2] IMPs comprise a significant fraction of the proteins encoded in an organism's genome. [3]
In 1972, S. Jonathan Singer and Garth Nicolson developed new ideas for membrane structure. Their proposal was the fluid mosaic model, which is one of the dominant models now. It has two key features—a mosaic of proteins embedded in the membrane, and the membrane being a fluid bi-layer of lipids.
Several integral nuclear membrane proteins of different size and structure have been identified. [3] It is proposed that they share some structural features with respect to nucleoplasmic domain(s) and lipid-soluble domain(s). Some INM proteins contain common protein domain structures, and can thus be categorised into known protein domain families.
The Membrane Protein Structural Dynamics Consortium (MPSDC) is a large scale collaborative consortium composed of an interdisciplinary team of scientists who use biophysical and computational methods to understand how the structure and movement of membrane proteins determine their functions. [2]