Title : Non-alpha-helical elements modulate polytopic membrane protein architecture.

Pub. Date : 2001 Feb 16

PMID : 11237604






1 Functional Relationships(s)
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1 Using both existing and newly developed tools to analyze transmembrane segments of all available membrane protein three-dimensional structures, including that very recently elucidated for the GPCR, rhodopsin, we report here the finding of frequent non-alpha-helical components, i.e. 3(10)-helices ("tight turns"), pi-helices ("wide turns") and intrahelical kinks (often due to residues other than proline). Proline rhodopsin Homo sapiens