Revisão Revisado por pares

Dynamics in Rhodopsin

2002; Wiley; Volume: 3; Issue: 10 Linguagem: Galês

10.1002/1439-7633(20021004)3

ISSN

1439-7633

Autores

Judith Klein‐Seetharaman,

Tópico(s)

Molecular spectroscopy and chirality

Resumo

ChemBioChemVolume 3, Issue 10 p. 981-986 Minireview Dynamics in Rhodopsin Judith Klein-Seetharaman Prof., Judith Klein-Seetharaman Prof. [email protected] Department of Pharmacology University of Pittsburgh School of Medicine E1355 Biomedical Science Tower Pittsburgh, PA 15261 (USA) Fax: (+1) 412-648-1945Search for more papers by this author Judith Klein-Seetharaman Prof., Judith Klein-Seetharaman Prof. [email protected] Department of Pharmacology University of Pittsburgh School of Medicine E1355 Biomedical Science Tower Pittsburgh, PA 15261 (USA) Fax: (+1) 412-648-1945Search for more papers by this author First published: 01 October 2002 https://doi.org/10.1002/1439-7633(20021004)3:10 3.0.CO;2-9Citations: 19Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat Abstract Dancing in the dark: Much is known about the structure and light-induced conformational changes of the mammalian dim-light receptor rhodopsin, a model system for the entire G-protein-coupled receptor family. Less attention has been paid to the dynamic properties of rhodopsin. Growing evidence for the presence of large backbone motions in the inactive dark-state conformation of rhodopsin and their importance for the functional, light-induced conformational changes necessary for signal transduction are reviewed here. Cysteine mutagenesis experiments and spectroscopic techniques are combined to reveal more information about the protein dynamics. References 1 H. G. Khorana, J. Biomol. Struct. Dyn. 2000, 11, 1–16. 10.1080/07391102.2000.10506598 Google Scholar 2 K. Palczewski, T. Kumasaka, T. Hori, C. A. Behnke, H. Motoshima, B. A. Fox, I. LeTrong, D. C. Teller, T. Okada, R. E. Stenkamp, M. 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