Methodology article
Prediction of transmembrane helix orientation in polytopic membrane proteins
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* Corresponding author: Larisa Adamian larisa@uic.edu
Department of Bioengineering, University of Illinois at Chicago, M/C 563, 835 S. Wolcott St, Chicago, IL 60612-7340, USA
BMC Structural Biology 2006, 6:13 doi:10.1186/1472-6807-6-13
Published: 22 June 2006Additional files
Additional File 1:
Comparison of the failed predicted vs. correct buried faces. The correct faces have significant overlap with the predicted faces and differ only by one residue slide (rotation) of the helical wheel in 28 helices, and by two residue slides in 18 helices.
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Additional File 2:
Multiple sequence alignments for PetG, PetL, PetM, and PetN TM helices of cytochrome b6f. The first sequence in every sequence alignment is from 1Q90 structure, while the second sequence is from 1VF5 structure. Helix boundaries are based on 1Q90 structure assignment.
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