Peptides as transmembrane segments: decrypting the determinants for helix-helix interactions in membrane proteins.

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 alpha-helical transmembrane segments one with another to form the final functional protein structure. Peptides derived from the sequences of native alpha-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.

journal_name

Biopolymers

journal_title

Biopolymers

authors

Rath A,Johnson RM,Deber CM

doi

10.1002/bip.20668

subject

Has Abstract

pub_date

2007-01-01 00:00:00

pages

217-32

issue

2

eissn

0006-3525

issn

1097-0282

journal_volume

88

pub_type

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