Protein structure in membrane domains.

Abstract:

:Of great interest to the academic and pharmaceutical research communities, helical transmembrane proteins are characterized by their ability to dissolve and fold in lipid bilayers--properties conferred by polypeptide spans termed transmembrane domains (TMDs). The apolar nature of TMDs necessitates the use of membrane-mimetic solvents for many structure and folding studies. This review examines the relationship between TMD structure and solvent environment, focusing on principles elucidated largely in membrane-mimetic environments with single-TMD protein and peptide models. Following a brief description of TMD sequence and conformational characteristics gleaned from the structural database, we present an overview of the conceptual models used to study folding in vitro. The impact of sequence and solvent context on the incorporation of TMDs into membranes, and its role in measurements of TMD self-assembly strengths, is then described. We conclude with a discussion of the nonspecific effects of membrane components on TMD stability.

journal_name

Annu Rev Biophys

authors

Rath A,Deber CM

doi

10.1146/annurev-biophys-050511-102310

subject

Has Abstract

pub_date

2012-01-01 00:00:00

pages

135-55

eissn

1936-122X

issn

1936-1238

journal_volume

41

pub_type

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