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Structural features of transmembrane helices
Author(s) -
Hildebrand Peter Werner,
Preissner Robert,
Frömmel Cornelius
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00061-4
Subject(s) - ramachandran plot , dihedral angle , transmembrane domain , transmembrane protein , crystallography , globular protein , chemistry , protein structure , membrane protein , hydrogen bond , structural motif , lipid bilayer , helix (gastropod) , bilayer , biophysics , membrane , molecule , biology , biochemistry , ecology , receptor , organic chemistry , snail
A total of 160 transmembrane helices of 15 non‐homologous high‐resolution X‐ray protein structures have been analyzed in respect of their structural features. The dihedral angles and hydrogen bonds of the helical sections that span the hydrophobic interior of the lipid bilayer have been investigated. The Ramachandran plot of protein channels and solute transporters exhibit a significant shift Δ ( φ ‐ and ψ ‐angles) of Δ mean (+4.5° and −5.4°), compared to a reference group of 151 α‐helices of the same average length derived from water‐soluble globular proteins. At the C‐termini of transmembrane helices structural motifs equivalent to the Gly‐caps of helices in globular proteins have been found, with two third of the transmembrane Gly‐caps taking up a primary structure that is typically not found at helix termini exposed to a polar solvent. The structural particularities reported here are relevant for the three‐dimensional modelling of membrane protein structures.