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In the middle of the S6 helix in voltage-gated potassium channels there is a highly conserved Pro-Val-Pro motif, while the equivalent M2 helix of inward rectifier potassium channels contains a conserved glycine residue in a comparable position. The structural implications of these conserved motifs are of interest given the evidence that S6 and M2 are components of the lining of their respective pores. Multiple sequence alignment and TM helix prediction methods were used to define consensus regions for S6 and M2. Ensembles of 50 structures for each helix were generated by simulated annealing and restrained molecular dynamics. Time-dependent fluctuations of S6 and M2 were investigated by long time scale molecular dynamics simulations on representative members of each ensemble carried out in vacuo in the presence and absence of a hydrophobic potential that mimics a lipid bilayer. The results are discussed in terms of the structural basis of the kink in S6 and M2 and of a putative functional role for flexible helices as "molecular swivels."

Original publication

DOI

10.1002/(SICI)1097-0282(199610)39:4<503::AID-BIP3>3.0.CO;2-0

Type

Journal article

Journal

Biopolymers

Publication Date

10/1996

Volume

39

Pages

503 - 515

Keywords

Amino Acid Sequence, Conserved Sequence, Models, Molecular, Molecular Sequence Data, Potassium Channels, Protein Structure, Secondary, Static Electricity, Thermodynamics