Modeling transmembrane helical oligomers.
Recently, methods for the analysis and design of water-soluble, oligomeric bundles of alpha helices, including coiled coils, have reached a high level of sophistication. These same methods may now be applied to transmembrane helical bundles. Studies of the transmembrane domains of glycophorin, phospholamban, and the M2 protein from influenza A virus exemplify this general approach.
Dieckmann
G R
GR
Department of Biochemistry and Biophysics, Johnson Research Foundation, University of Pennsylvania School of Medicine, Philadelphia 19104-6059, USA. dieckman@crystal.med.upenn.edu
DeGrado
W F
WF
D002135:Calcium-Binding Proteins / Q000737:chemistry; D003198:Computer Simulation; D006021:Glycophorins / Q000737:chemistry; D009980:Influenza A virus / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D014763:Viral Matrix Proteins / Q000737:chemistry; D000099211:Phospholamban; D000086082:Viroporin Proteins
D002135:Calcium-Binding Proteins; D006021:Glycophorins; D008565:Membrane Proteins; D014763:Viral Matrix Proteins; D000099211:Phospholamban; C031540:M-protein, influenza virus; C488937:M2 protein, Influenza A virus; D000086082:Viroporin Proteins