Abstract
Membrane-spanning α-helices represent major sites of protein-protein interaction in membrane protein oligomerization and folding. As such, these interactions may be of exquisite specificity. Specificity often rests on a complex interplay of different types of residues forming the helix-helix interfaces via dense packing and different non-covalent forces, including van der Waal’s forces, hydrogen bonding, charge-charge interactions, and aromatic interactions. These interfaces often contain complex residue motifs where the contribution of constituent amino acids depends on the context of the surrounding sequence. Moreover, transmembrane helix-helix interactions are increasingly recognized as being dynamic and dependent on the functional state of a given protein.
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Langosch, D., Herrmann, J.R., Unterreitmeier, S., Fuchs, A. (2010). Helix-helix interaction patterns in membrane proteins. In: Structural Bioinformatics of Membrane Proteins. Springer, Vienna. https://doi.org/10.1007/978-3-7091-0045-5_10
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