Chapter title |
Analyzing the Effects of Hydrophobic Mismatch on Transmembrane α-Helices Using Tryptophan Fluorescence Spectroscopy.
|
---|---|
Chapter number | 5 |
Book title |
Membrane Proteins
|
Published in |
Methods in molecular biology, August 2013
|
DOI | 10.1007/978-1-62703-583-5_5 |
Pubmed ID | |
Book ISBNs |
978-1-62703-582-8, 978-1-62703-583-5
|
Authors |
Caputo GA, Gregory A. Caputo |
Abstract |
Hydrophobic matching between transmembrane protein segments and the lipid bilayer in which they are embedded is a significant factor in the behavior and orientation of such transmembrane segments. The condition of hydrophobic mismatch occurs when the hydrophobic thickness of a lipid bilayer is significantly different than the length of the membrane spanning segment of a protein, resulting in a mismatch. This mismatch can result in altered function of proteins as well as nonnative structural arrangements including effects on transmembrane α-helix tilt angles, oligomerization state, and/or the formation of non-transmembrane topographies. Here, a fluorescence-based protocol is described for testing model transmembrane α-helices and their sensitivity to hydrophobic mismatch by measuring the propensity of these helices to form non-transmembrane structures. Overall, good hydrophobic matching between the bilayer and transmembrane segments is an important factor that must be considered when designing membrane proteins or peptides. |
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