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David S. Goodsell, is an associate professor at the Scripps Research Institute [1] and research professor at Rutgers University, New Jersey [2] (joint appointment). He is especially known for his watercolor paintings of cell interiors. [3] [4] David S. Goodsell at the booth for the RCSB Protein Data Bank in 2013
He has authored several book chapters, and two books entitled, Membrane Protein Structure: Experimental Approaches and Cell Boundaries: How Membranes and Their Proteins Work. [ 3 ] White is a Fellow of the American Association for the Advancement of Science , [ 4 ] Neutron Scattering Society of America, [ 5 ] and Biophysical Society , where he ...
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]
David E. Green (1910–1983 ... who worked on the structure and function of blood proteins. ... known for work on membrane proteins and protein-nucleic acid complexes.
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.
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]
The technique allows insight on the nature of how a protein's structure and conformational changes create/form protein function. Andrew Huxley — mathematical theory of how ion fluxes produce nerve impulses (with Alan Hodgkin) Hugh Huxley (English, 1924–2013) — muscle structure and contraction
Tetraspanins are a family of membrane proteins found in all multicellular eukaryotes also referred to as the transmembrane 4 superfamily (TM4SF) proteins. These proteins have four transmembrane alpha-helices and two extracellular domains, one short (called the s mall e xtracellular d omain or l oop, SED/SEL or EC1) and one longer, typically 100 ...