Interhelical hydrogen bonding drives strong interactions in membrane proteins

@article{Zhou2000InterhelicalHB,
  title={Interhelical hydrogen bonding drives strong interactions in membrane proteins},
  author={Fang Xiao Zhou and Melanie J. Cocco and William P. Russ and Axel T Brunger and Donald M. Engelman},
  journal={Nature Structural Biology},
  year={2000},
  volume={7},
  pages={154-160}
}
Polar residues in transmembrane α-helices may strongly influence the folding or association of integral membrane proteins. To test whether a motif that promotes helix association in a soluble protein could do the same within a membrane, we designed a model transmembrane helix based on the GCN4 leucine zipper. We found in both detergent miscelles and biological membranes that helix association is driven strongly by asparagine, independent of the rest of the hydrophobic leucine and/or valine… CONTINUE READING
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