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J Mol Biol. 1997 Oct 10;272(5):780-9.

Helix packing in membrane proteins.

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Department of Chemistry and Biochemistry, UCLA-DOE 90095-1570, USA.


A survey of 45 transmembrane (TM) helices and 88 helix packing interactions in three independent transmembrane protein structures reveals the following features. (1) Helix lengths range from 14 to 36 residues with an average length of 26.4 residues. There is a preference for lengths greater than 20 residues. (2) The helices are tilted with respect to the bilayer normal by an average of 21 degrees, but there is a decided preference for smaller tilt angles. (3) The distribution of helix packing angles is very different than for soluble proteins. The most common packing angles for TM helices are centered around +20 degrees while for soluble proteins packing angles of around -35 degrees are the most prevalent. (4) The average distance of closest approach is 9.6 A, which is the same as soluble proteins. (5) There is no preference for the positioning of the point of closest approach along the length of the helices. (6) It is almost a rule that TM helices pack against neighbors in the sequence. Of the 37 helices that have a sequence neighbor, 36 of them are in significant contact with a neighbor. (7) An antiparallel orientation is more prevalent than a parallel orientation and antiparallel interactions are more intimate on average. The general features of helix bundle membrane protein architecture described in this survey should prove useful in the modeling of helix bundle transmembrane proteins.

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