2015年2月11日 · The simulations indicate that the strictly conserved Y169 in mammalian prion proteins stabilizes the 3 10 -helical turn in the β2-α2 loop, thus hindering the conversion to an aggregation-prone conformation.

2015年12月21日 · Here we analyze the role of a tyrosine residue (Y169) which is strictly conserved in mammalian PrPs. Nuclear magnetic resonance (NMR) spectroscopy studies of many mammalian PrP C proteins have provided evidence of a conformational equilibrium between a 3 10 -helical turn and a type I β turn conformation in …

Interactions of Y169 in the 3 10 -helical turn conformation of the b2-a2 loop. (Left) The X-ray structure of mouse PrP (PDB code 4H88) is shown by a ribbon model. The residues mentioned in the...

2015年11月2日 · Here we analyze the role of a tyrosine residue (Y169) which is strictly conserved in mammalian PrPs. Nuclear magnetic resonance (NMR) spectroscopy studies of many mammalian PrPC proteins have...

We hypothesized that the Y169G mutation would facilitate the rearrangement of the β2-α2 loop because of the loss of favorable interactions between the Y169 side chain and residues F175 and D178 (Figure 1, top right), as well as the reduced steric hindrance of glycine.

SSR code A6000 has been allocated for use by the RPAS operating BVLOS in segregated airspace. SSR code is to be treated as unvalidated and unverified. The activation status of EGTS496A will be available during the hours of watch, from Aberdeen Radar on channel 119.055.

Here we analyze the role of a tyrosine residue (Y169) which is strictly conserved in mammalian PrPs. Nuclear magnetic resonance (NMR) spectroscopy studies of many mammalian PrP (C) proteins have provided evidence of a conformational equilibrium between a 3 (10)-helical turn and a type I β turn conformation in the β2-α2 loop (residues 165-175).

2015年2月11日 · The transition of the β2-α2 loop to β turn increases the solvent-exposure of the hydrophobic stretch 169-YSNQNNF-175. The simulations indicate that the strictly conserved Y169 in mammalian prion proteins stabilizes the 3 10 -helical turn in the β2-α2 loop, thus hindering the conversion to an aggregation-prone conformation.

2006年1月9日 · Phenylalanine replacement of Y169 (PLD2 Y169F) or Y179 (PLD2 Y179F) reduced Grb2 binding while simultaneous mutation completely abolished it.

2015年9月16日 · Here we analyze the role of a tyrosine residue (Y169) which is strictly conserved in mammalian PrPs. Nuclear magnetic resonance (NMR) spectroscopy studies of many mammalian PrPCproteins have provided evidence of a conformational equilibrium between a 310-helical turn and a type I turn conformation. in the 2- 2 loop (residues 165–175).