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
Biopolymersjournal_title
Biopolymersauthors
Rath A,Johnson RM,Deber CMdoi
10.1002/bip.20668subject
Has Abstractpub_date
2007-01-01 00:00:00pages
217-32issue
2eissn
0006-3525issn
1097-0282journal_volume
88pub_type
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