Structure of membrane-embedded M13 major coat protein is insensitive to hydrophobic stress.

Abstract:

:The structure of a membrane-embedded alpha-helical reference protein, the M13 major coat protein, is characterized under different conditions of hydrophobic mismatch using fluorescence resonance energy transfer in combination with high-throughput mutagenesis. We show that the structure is similar in both thin (14:1) and thick (20:1) phospholipid bilayers, indicating that the protein does not undergo large structural rearrangements in response to conditions of hydrophobic mismatch. We introduce a "helical fingerprint" analysis, showing that amino acid residues 1-9 are unstructured in both phospholipid bilayers. Our findings indicate the presence of pi-helical domains in the transmembrane segment of the protein; however, no evidence is found for a structural adaptation to the degree of hydrophobic mismatch. In light of current literature, and based on our data, we conclude that aggregation (at high protein concentration) and adjustment of the tilt angle and the lipid structure are the dominant responses to conditions of hydrophobic mismatch.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Vos WL,Schor M,Nazarov PV,Koehorst RB,Spruijt RB,Hemminga MA

doi

10.1529/biophysj.107.112698

subject

Has Abstract

pub_date

2007-11-15 00:00:00

pages

3541-7

issue

10

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(07)71605-3

journal_volume

93

pub_type

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