Translocons, thermodynamics, and the folding of membrane proteins.

Abstract:

:Recent three-dimensional structures of helical membrane proteins present new challenges for the prediction of structure from amino acid sequence. Membrane proteins reside stably in a thermodynamic free energy minimum after release into the membrane's bilayer fabric from the translocon complex. This means that structure prediction is primarily a problem of physical chemistry. But the folding processes within the translocon must also be considered. A distilled overview of the physical principles of membrane protein stability is presented, and extended to encompass translocon-assisted folding.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

White SH

doi

10.1016/s0014-5793(03)01153-0

keywords:

subject

Has Abstract

pub_date

2003-11-27 00:00:00

pages

116-21

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014579303011530

journal_volume

555

pub_type

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