Peptides as transmembrane segments: Decrypting the determinants for helix–helix interactions in membrane proteins
✍ Scribed by Arianna Rath; Rachel M. Johnson; Charles M. Deber
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2007
- Tongue
- English
- Weight
- 548 KB
- Volume
- 88
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
Although the structural analysis of membrane proteins is advancing, an understanding of the basic principles that underlie their folding and assembly remains limited because of the high insolubility intrinsic to these molecules and concomitant challenges in obtaining crystals. Fortunately, from an experimental standpoint, membrane protein folding can be approximated as the rigid‐body docking of pre‐formed α‐helical transmembrane segments one with another to form the final functional protein structure. Peptides derived from the sequences of native α‐helical transmembrane segments and those that mimic their properties are therefore valuable in the experimental evaluation of protein folding within the membrane. Here we present an overview of the progress made in our laboratory and elsewhere in using peptide models toward defining the sequence requirements and forces stabilizing membrane protein folds. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 88: 217–232, 2007.
This article was originally published online as an accepted preprint. The ‘Published Online’ date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at [email protected]