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 Jjournal_title
Biophysical journalauthors
Vos WL,Schor M,Nazarov PV,Koehorst RB,Spruijt RB,Hemminga MAdoi
10.1529/biophysj.107.112698subject
Has Abstractpub_date
2007-11-15 00:00:00pages
3541-7issue
10eissn
0006-3495issn
1542-0086pii
S0006-3495(07)71605-3journal_volume
93pub_type
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