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The hydrogen-bonding network of water molecules and the peptide backbone in the region connecting Asp83, Gly120, and Glu113 in bovine rhodopsin.
Nagata T, Terakita A, Kandori H, Shichida Y, Maeda A. Nagata T, et al. Among authors: kandori h. Biochemistry. 1998 Dec 8;37(49):17216-22. doi: 10.1021/bi9810149. Biochemistry. 1998. PMID: 9860835
The pigments studied were single and combined mutants of intramembrane residues of bovine rhodopsin: Asp83, Glu113, Gly120, Gly121, and Glu122. Previous studies [Nagata, T., Terakita, A., Kandori, H., Kojima, D., Shichida, Y., and Maeda, A. (1997) Biochemistry 36, 6 …
The pigments studied were single and combined mutants of intramembrane residues of bovine rhodopsin: Asp83, Glu113, Gly120, Gly121, and Glu1 …
Structural changes in the Schiff base region of squid rhodopsin upon photoisomerization studied by low-temperature FTIR spectroscopy.
Ota T, Furutani Y, Terakita A, Shichida Y, Kandori H. Ota T, et al. Among authors: kandori h. Biochemistry. 2006 Mar 7;45(9):2845-51. doi: 10.1021/bi051937l. Biochemistry. 2006. PMID: 16503639
On the basis of these results, we propose that squid rhodopsin possesses a "bridge" water between the Schiff base and its counterion as well as squid retinochrome [Furutani, Y., Terakita, A., Shichida, Y., and Kandori, H. (2005) Biochemistry 44, 7988-7997], which is …
On the basis of these results, we propose that squid rhodopsin possesses a "bridge" water between the Schiff base and its counterion as well …
An FTIR study of monkey green- and red-sensitive visual pigments.
Katayama K, Furutani Y, Imai H, Kandori H. Katayama K, et al. Among authors: kandori h. Angew Chem Int Ed Engl. 2010;49(5):891-4. doi: 10.1002/anie.200903837. Angew Chem Int Ed Engl. 2010. PMID: 20052695 No abstract available.
380 results