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B. de Kruijff

Researcher at Utrecht University

Publications -  204
Citations -  17134

B. de Kruijff is an academic researcher from Utrecht University. The author has contributed to research in topics: Bilayer & Vesicle. The author has an hindex of 71, co-authored 204 publications receiving 16788 citations. Previous affiliations of B. de Kruijff include ETH Zurich & Laboratory of Molecular Biology.

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Journal ArticleDOI

Size and orientation of the lipid II headgroup as revealed by AFM imaging.

TL;DR: The size and orientation of the bacterial Lipid II (L II) headgroup when the L II molecule is present in liquid-crystalline domains of DOPC in a supported DPPC bilayer is investigated and a model for the orientation ofThe L II headgroup in the membrane is proposed.
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Lipid dependence of glycophorin-induced transbilayer movement of lysophosphatidylcholine in large unilamellar vesicles

TL;DR: In vesicles made of the total erythrocyte lipids (phospholipids and cholesterol) glycophorin does not facilitate the lysophosphatidylcholine transbilayer movement, suggesting that a complex mixture of lipids is required to properly seal the lipid-protein interface.
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Characterization of the Import Process of a Transit Peptide into Chloroplasts

TL;DR: The import of the full-length transit peptide of ferredoxin was investigated, and it was found that the initial binding of precursor proteins may be facilitated by transit sequence-lipid interactions.
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Interactions of mitochondrial precursor protein apocytochrome c with phosphatidylserine in model membranes. A monolayer study.

TL;DR: It is concluded that the charge interactions are required for binding and penetration of the protein and cholesterol can enhance the protein binding.
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Anionic phospholipids can mediate membrane insertion of the anionic part of a bound peptide

TL;DR: It is demonstrated that the negatively charged membrane surface of mixed phosphatidylcholine/phosph atidylglycerol small unilamellar vesicles enhances the protonation of the C‐terminal carboxyl group, and the subsequent insertion of that part of the peptide.