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I agree with Ruud. That is a typical amphipathic helical arrangement. Cheers, Chris -- Christopher L. Colbert, Ph.D. Associate Professor Department of Chemistry and Biochemistry North Dakota State University P.O. Box 6050 Dept. 2710 Fargo, ND 58108-6050 PH: (701) 231-7946 FAX: (701) 231-8324 From: CCP4 bulletin board <[log in to unmask]<mailto:[log in to unmask]>> on behalf of Ruud Hovius <[log in to unmask]<mailto:[log in to unmask]>> Reply-To: Ruud Hovius <[log in to unmask]<mailto:[log in to unmask]>> Date: Saturday, March 3, 2018 at 5:50 PM To: "[log in to unmask]<mailto:[log in to unmask]>" <[log in to unmask]<mailto:[log in to unmask]>> Subject: Re: [ccp4bb] A helix with leucine repeats an amphiphatic helix ? if so a classical motif of membrane binding peptides Best greetings, Ruud On 3/3/18 21:51, Cheng Zhang wrote: Hi all, We recently got a structure of a transmembrane protein. There is a helix that is parallel to the membrane. The function of this helix is not known and we are trying to make some hypothesis. A unique feature is that there are repeated leucine residues on this helix facing the lipids. I am wondering if anyone has seen a similar pattern and could suggest possible function, e.g. membrane anchoring? Thanks! Best, Cheng [cid:part1.B5B5C011.C9B361F1@epfl.ch] -- --------------------- Cheng Zhang -- Ruud Hovius EPFL SB ISIC LCBM Office CH B3 424 CH-1015 Lausanne +41-21-693-3134 http://people.epfl.ch/ruud.hovius