H
H. Gobind Khorana
Researcher at Massachusetts Institute of Technology
Publications - 97
Citations - 7174
H. Gobind Khorana is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Rhodopsin & Bacteriorhodopsin. The author has an hindex of 39, co-authored 97 publications receiving 6995 citations. Previous affiliations of H. Gobind Khorana include Weizmann Institute of Science & University of Pittsburgh.
Papers
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Journal ArticleDOI
Requirement of Rigid-Body Motion of Transmembrane Helices for Light Activation of Rhodopsin
TL;DR: Disulfide cross-linking of the helices prevented activation of transducin, which suggests the importance of this movement for activation of rhodopsin.
Journal ArticleDOI
Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
TL;DR: The toxic constitutively active rhodopsin mutant, E113Q/E134Q/M257Y, previously shown to require inducible expression, has now been expressed in an HEK293S GNTI−-inducible cell line at levels comparable with those obtained with WT rhodopin.
Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin (transmembrane receptor/site-directed mutagenesis/retinal chromophore/visual pigment/synthetic gene)
TL;DR: In this paper, a site-directed mutagenesis was used to replace charged amino acids in bovine rhodopsin transmembrane helix C with substituted amino acids.
Journal ArticleDOI
Structure and Function in Rhodopsin MEASUREMENT OF THE RATE OF METARHODOPSIN II DECAY BY FLUORESCENCE SPECTROSCOPY
TL;DR: In this paper, an increase in fluorescence was observed upon light activation of bovine rhodopsin and the rate of increase is monoexponential (t 1/2 = 15.5 min) at 20°C in 0.1% dodecyl maltoside at pH 6.0.
Book ChapterDOI
Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking.
TL;DR: In this article, the authors presented rhodopsin structure and dynamics at the cytoplasmic face in solution, the comparison between the solution structure and the crystal structure, and the structural changes underlying receptor activation.