Understanding peptide interactions with the lipid bilayer: a guide to membrane protein engineering |
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Authors: | Bechinger B |
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Institution: | Max-Planck-Institut für Biochemie, Am Klopferspitz 18A, D-82152, Martinsried, Germany. bechinge@biochem.mpg.de |
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Abstract: | In recent years, studies of the interactions of designed hydrophobic and amphipathic polypeptides with biological membranes have progressed considerably. In-plane and transmembrane helical domains have been engineered as well as sequences that exhibit dynamic distributions of different topologies. These sequences not only help our understanding of the thermodynamic interaction contributions that determine peptide orientation, but also exhibit interesting biological functions as autonomous units. In addition, helices are considered to be folding intermediates of multi-spanning membrane proteins. The specificity and thermodynamic stability of transmembrane helix-helix interactions or the assembly of beta sheets at the membrane surface have, therefore, become a focus of ongoing research. |
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Keywords: | Lipid bilayer membrane proteins peptides transmembrane helices |
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