Sequence motifs, polar interactions and conformational changes in helical membrane proteins.

Abstract:

:The alpha helices of transmembrane proteins interact to form higher order structures. These interactions are frequently mediated by packing motifs (such as GxxxG) and polar residues. Recent structural data have revealed that small sidechains are able to both stabilize helical membrane proteins and allow conformational changes in the structure. The strong interactions involving polar sidechains often contribute to protein misfolding or malfunction.

journal_name

Curr Opin Struct Biol

authors

Curran AR,Engelman DM

doi

10.1016/s0959-440x(03)00102-7

subject

Has Abstract

pub_date

2003-08-01 00:00:00

pages

412-7

issue

4

eissn

0959-440X

issn

1879-033X

pii

S0959440X03001027

journal_volume

13

pub_type

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