Wayne L. Hubbell | |
---|---|
Born | March 24, 1943 |
Nationality | American |
Education | Oregon State University, B.S. 1965: Stanford University (Ph.D. 1970); Stanford University (Postdoctoral Fellow) |
Known for | Site-directed spin labeling |
Scientific career | |
Fields | Biochemistry of vision |
Institutions | University of California, Los Angeles thesis_title = |
Doctoral students | Linda Columbus |
This article includes a list of references, related reading, or external links, but its sources remain unclear because it lacks inline citations .(February 2013) |
Wayne L. Hubbell (born 24 March 1943) is an American biochemist and member of the National Academy of Sciences. He is Professor of Biochemistry and Jules Stein Professor of Ophthalmology at the University of California, Los Angeles. His research focuses on the visual system, and is primarily supported by a grant from the National Eye Institute.[ citation needed ]
Dr. Hubbell has studied the relationship between the molecular structure of protein and the conformational changes that control its function. Of particular interest are membrane proteins that behave as "molecular switches", i.e., proteins whose structures are switched to an active state by a physical or chemical signals. An example is light-activated rhodopsin, the visual pigment in photoreceptor cells of the retina. The goal is to elucidate the structure of rhodopsin, the mechanism of the molecular switch, and regulation of this switch by associated proteins, transducin and arrestin.
Dr. Hubbell's research also includes structure and function relationships in water-soluble proteins such as the lens protein, a-crystallin, and the retinoid carrying proteins which transport vitamin A throughout photoreceptor cells.
Dr. Hubbell's laboratory developed site-directed spin labeling (SDSL), a technique for the exploration of protein structure and dynamics. By changing the genetic code, a specific attachment point in the protein is created for a nitroxide spin label probe. Analysis of the electron paramagnetic resonance (EPR) spectrum of the spin label provides information about the local environment in the protein. With a sufficiently large set of labeled proteins, global information on structure is obtained, and most importantly, changes in the structure during function can be followed in real time.
Transducin (Gt) is a protein naturally expressed in vertebrate retina rods and cones and it is very important in vertebrate phototransduction. It is a type of heterotrimeric G-protein with different α subunits in rod and cone photoreceptors.
Christian Boehmer Anfinsen Jr. was an American biochemist. He shared the 1972 Nobel Prize in Chemistry with Stanford Moore and William Howard Stein for work on ribonuclease, especially concerning the connection between the amino acid sequence and the biologically active conformation.
Site-directed spin labeling (SDSL) is a technique for investigating the structure and local dynamics of proteins using electron spin resonance. The theory of SDSL is based on the specific reaction of spin labels with amino acids. A spin label's built-in protein structure can be detected by EPR spectroscopy. SDSL is also a useful tool in examinations of the protein folding process.
David S. Cafiso is an American biochemist and a professor of chemistry at the University of Virginia. His research focuses on membrane proteins and cell signaling, and is primarily supported by grants from the National Institute of Health.
Rhodopsin kinase is a serine/threonine-specific protein kinase involved in phototransduction. This enzyme catalyses the following chemical reaction:
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Paul Hargrave is an American biochemist whose laboratory work established key features of the structure of rhodopsin.
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