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Conformational analysis of fragment of human Pin1 ww domain: influence of charged amino-acid residues on β-hairpin structure

Makowska J., Uber D., Żmudzińska W., Chmurzyński L.

TASK Quarterly : scientific bulletin of Academic Computer Centre in Gdansk

2014

Vol. 18, No 4

343--349

We examined the effect of like-charged residues on the conformation of an original nine amino-acid-residue fragment of the human Pin1 WW domain (hPin1) with the f ollowing sequence: Ac-Arg-Met-Ser-Arg-Ser-Ser-Gly-Arg-Val-NH 2 (U9). This was facilitated by CD and NMR spectroscopic measurements, and molecular dynamics calculations. Our ear lier studies suggested that the presence of like-charged residues at the end of a shor t polypeptide chain composed of nonpolar residues could induce a chain reversal. For the U9 pep tide, canonical MD simulations with NMR -derived restraints demonstrated the presence of ensembles of stru ctures with a tendency to form a β -chain reversal. Additionally, thermal stabilities of the peptide und er study were measured using differential scanning calorimetry ( DSC ). The estimated well defined phase transition point showed that conformational equilibria in the U9 pe ptide were strongly dependent on temperature.

The study on helix-inducing propensity of A-hydroxymethylserine based on the host-guest approach

Lisowski M., Stasiak M., Leplawy M.

Polish Journal of Chemistry

1999

vol. 73 nr 2

313-319

The solid phase synthesis of a-hydroxymethylserine peptides is affected by accumulation of deleted sequences and NŽO-acyl migrations, occurring under acidic conditions of cleavage from Wang resin. The conformational behaviour of peptides, containing alanine host-residues separated by a single or consecutive a-hydroxymethylserine (HmS) guest-residues, has been studied by CD spectroscopy in polar protic solvents. The presence of sequential motif (Ala-HmS)n, n=2,4, shifts the conformational equilibria towards ordered structures. The CD spectrum of the nonapeptide Ac-Ala-(HmS-Ala)4-OH in trifluoroethanol is indicative of a right-handed helix. Peptides with consecutive HmSn residues, n=2,3, are apparently less ordered than those containing alternating sequences Ala-HmS. Random coil conformation is adopted by the nonapeptide Ac-Ala3-(HmS)3-Ala-OH containing three neighbouring HmS residues.