Modelling the structures of G protein-coupled receptors aided by three-dimensional validation

BMC Bioinformatics

Table 2 Average hydrophobicity and hydrophobicity moment of the transmembrane helices (I–VII) of hGalR1 based on the sequence alignment proposed by Baldwin et al. [3].

TMS^a	Number of residues	Average hydrophobicity^b	Hydrophobic moment^c	Alpha phase^d
I	27	0.68	0.06	239
II	27	0.38	0.18	157
III	35	0.47	0.17	17
IV	25	0.37	0.13	222
V	30	0.44	0.21	115
VI	30	0.38	0.09	339
VII	24	0.22	0.25	198

^aTransmembrane segment.
^bThe hydrophobicity scale used in these calculations was the consensus scale of Eisenberg et al. [41].
^cMean vector sum of the hydrophobicities of the side chains of the helix.
^dThe angle of the moment from the first residue in the window, in the direction in which the α-helix turns.

ISSN: 1471-2105