Analyzing the effects of hydrophobic mismatch on transmembrane α-helices using tryptophan fluorescence spectroscopy

Research output: Chapter in Book/Report/Conference proceedingChapter

4 Scopus citations

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 fl uorescence-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 nontransmembrane 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.

Original languageEnglish (US)
Title of host publicationMembrane Proteins
Subtitle of host publicationFolding, Association, and Design
PublisherHumana Press Inc.
Pages95-116
Number of pages22
ISBN (Print)9781627035828
DOIs
StatePublished - Jan 1 2013

Publication series

NameMethods in Molecular Biology
Volume1063
ISSN (Print)1064-3745

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics

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    Caputo, G. A. (2013). Analyzing the effects of hydrophobic mismatch on transmembrane α-helices using tryptophan fluorescence spectroscopy. In Membrane Proteins: Folding, Association, and Design (pp. 95-116). (Methods in Molecular Biology; Vol. 1063). Humana Press Inc.. https://doi.org/10.1007/978-1-62703-583-5_5