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Synthetic peptides as models for intrinsic membrane proteins
Authors:Killian J Antoinette
Institution:Department of Biochemistry of Membranes, Center for Biomembranes and Lipid Enzymology, Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands. j.a.kilian@chem.uu.nl
Abstract:There are many ways in which lipids can modulate the activity of membrane proteins. Simply a change in hydrophobic thickness of the lipid bilayer, for example, already can have various consequences for membrane protein organization and hence for activity. By using synthetic transmembrane peptides, it could be established that these consequences include peptide oligomerization, tilt of transmembrane segments, and reorientation of side chains, depending on the specific properties of the peptides and lipids used. The results illustrate the potential of the use of synthetic model peptides to establish general principles that govern interactions between membrane proteins and surrounding lipids.
Keywords:Transmembrane peptide  α-Helix  Hydrophobic mismatch  Interfacial anchoring  Snorkeling  Tryptophan
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