motilin and tetramethylsilane

motilin has been researched along with tetramethylsilane* in 1 studies

Other Studies

1 other study(ies) available for motilin and tetramethylsilane

Article	Year
Motilin-bicelle interactions: membrane position and translational diffusion. FEBS letters, 2003, Jun-19, Volume: 545, Issue:2-3 The interaction between the peptide hormone motilin and bicelles has been investigated by pulsed field gradient-nuclear magnetic resonance methods and by the use of paramagnetic probes. Diffusion coefficients were measured for motilin, the phospholipids with and without motilin, and for tetramethylsilane. The results show that around 90% of motilin is bound to acidic bicelles and 84% of motilin is bound to neutral bicelles. It is found that the apparent bicelle size is reduced by the presence of motilin. This cannot be explained by changes in 1,2-dihexanoyl-sn-glycero-3-phosphatidylcholine solubility. The use of paramagnetic agents to investigate the position of motilin shows that the turn in the N-terminus of motilin is inserted into the bicelle, while the helix most likely resides within the head-group layer. Topics: Circular Dichroism; Diffusion; Electron Spin Resonance Spectroscopy; Hydrogen-Ion Concentration; Lipid Bilayers; Membrane Lipids; Models, Molecular; Motilin; Nuclear Magnetic Resonance, Biomolecular; Phospholipids; Silanes; Solutions; Trimethylsilyl Compounds	2003

Article

Year

Motilin-bicelle interactions: membrane position and translational diffusion.

FEBS letters, 2003, Jun-19, Volume: 545, Issue:2-3

The interaction between the peptide hormone motilin and bicelles has been investigated by pulsed field gradient-nuclear magnetic resonance methods and by the use of paramagnetic probes. Diffusion coefficients were measured for motilin, the phospholipids with and without motilin, and for tetramethylsilane. The results show that around 90% of motilin is bound to acidic bicelles and 84% of motilin is bound to neutral bicelles. It is found that the apparent bicelle size is reduced by the presence of motilin. This cannot be explained by changes in 1,2-dihexanoyl-sn-glycero-3-phosphatidylcholine solubility. The use of paramagnetic agents to investigate the position of motilin shows that the turn in the N-terminus of motilin is inserted into the bicelle, while the helix most likely resides within the head-group layer.

Topics: Circular Dichroism; Diffusion; Electron Spin Resonance Spectroscopy; Hydrogen-Ion Concentration; Lipid Bilayers; Membrane Lipids; Models, Molecular; Motilin; Nuclear Magnetic Resonance, Biomolecular; Phospholipids; Silanes; Solutions; Trimethylsilyl Compounds

2003