Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 361130
Title Structure of membrane embedded M13 major coat protein is insensitive to hydrophobic stress
Author(s) Vos, W.L.; Schor, M.; Nazarov, P.V.; Koehorst, R.B.M.; Spruijt, R.B.; Hemminga, M.A.
Source Biophysical Journal 93 (2007)10. - ISSN 0006-3495 - p. 3541 - 3547.
DOI https://doi.org/10.1529/biophysj.107.112698
Department(s) Biophysics
EPS-2
Publication type Refereed Article in a scientific journal
Publication year 2007
Keyword(s) lipid-bilayer - molecular-dynamics - alpha-helices - model - mismatch - conformation - modulation - fret - aggregation - association
Abstract The structure of a membrane-embedded -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 -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.
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