TY - JOUR
T1 - Helical membrane proteins
T2 - Diversity of functions in the context of simple architecture
AU - Ubarretxena-Belandia, I.
AU - Engelman, D. M.
N1 - Funding Information:
We would like to thank Kakoli Mitra for critical reading of the manuscript and insightful discussions, and Fang Zhou, Alessandro Senes and members of the Engelman laboratory for helpful discussions. IUB was funded by a postdoctoral grant from the Basque Government. DME thanks the National Institutes of Health and National Science Foundation for support.
PY - 2001/6/1
Y1 - 2001/6/1
N2 - During the past year, research on helical membrane proteins has brought insights into the use of deviations from canonical α-helical conformation to support function and the further investigation of the sequestration of protein regions from the lipid bilayer to enhance these structural alternatives. Also, the structural roles of polar sidechains, the identification of motifs in helix interactions and the significance of certain topologies on a genome-wide scale have been further explored.
AB - During the past year, research on helical membrane proteins has brought insights into the use of deviations from canonical α-helical conformation to support function and the further investigation of the sequestration of protein regions from the lipid bilayer to enhance these structural alternatives. Also, the structural roles of polar sidechains, the identification of motifs in helix interactions and the significance of certain topologies on a genome-wide scale have been further explored.
UR - http://www.scopus.com/inward/record.url?scp=0035367173&partnerID=8YFLogxK
U2 - 10.1016/S0959-440X(00)00217-7
DO - 10.1016/S0959-440X(00)00217-7
M3 - Review article
C2 - 11406389
AN - SCOPUS:0035367173
SN - 0959-440X
VL - 11
SP - 370
EP - 376
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 3
ER -