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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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13C-NMR detection of lipid polymorphism in model and biological membranes

TL;DR: In this paper, the 13C-NMR line-width of various resonances of the lipid molecule and sensitive to the bilayer in equilibrium hexagonal and the bilayers in equilibrium 'isotropic' phase transition is described.
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Influence of glycophorin incorporation on Ca2+-induced fusion of phosphatidylserine vesicles.

TL;DR: The inhibition of Ca2+-induced fusion of PS vesicles by incorporation of glycophorin is explained by a combination of steric hindrance and electrostatic repulsion between the vesicle contents and a direct bilayer stabilization by the intramembranous hydrophobic part of the glycoph orin molecule.
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The specificity of monoglyceride–protein interactions and mechanism of the protein induced L β to coagel phase transition

TL;DR: The results show that lysozyme inserts efficiently into all monolayers tested, including pure monoglyceride layers, and a large exothermic binding enthalpy was observed which was found to depend on the nature of the monoglycersides but not of the proteins.
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The N-terminal half of a mitochondrial presequence peptide inserts into cardiolipin-containing membranes. Consequences for the action of a transmembrane potential.

TL;DR: It was found that membrane potential‐dependent protection from trypsin was much faster for the peptide bound to PG‐containing vesicles compared to CL‐containing membranes, suggesting that in the mitochondrial protein import process other components of the import apparatus are involved in the efficient potential‐driven translocation of presequences across the inner mitochondrial membrane.
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Influence of acylation on the channel characteristics of gramicidin A.

TL;DR: Channels formed by the acylgramicidins and by gramicidin A are structurally and conformationally equivalent, which means that lauroyl- and stearoylgramicIDin are approximately 200 times less effective in channel formation as compared to gramicidein A.