- Tytuł:
- Conformational analysis of fragment of human Pin1 ww domain: influence of charged amino-acid residues on β-hairpin structure
- Autorzy:
-
Makowska, J.
Uber, D.
Żmudzińska, W.
Chmurzyński, L. - Powiązania:
- https://bibliotekanauki.pl/articles/1935818.pdf
- Data publikacji:
- 2014
- Wydawca:
- Politechnika Gdańska
- Tematy:
-
peptide conformation
β-hairpin
hPin1 protein
NMR - Opis:
- 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 following 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 short polypeptide chain composed of nonpolar residues could induce a chain reversal. For the U9 peptide, canonical MD simulations with NMR -derived restraints demonstrated the presence of ensembles of structures with a tendency to form a β -chain reversal. Additionally, thermal stabilities of the peptide under study were measured using differential scanning calorimetry ( DSC ). The estimated well defined phase transition point showed that conformational equilibria in the U9 peptide were strongly dependent on temperature.
- Źródło:
-
TASK Quarterly. Scientific Bulletin of Academic Computer Centre in Gdansk; 2014, 18, 4; 343--349
1428-6394 - Pojawia się w:
- TASK Quarterly. Scientific Bulletin of Academic Computer Centre in Gdansk
- Dostawca treści:
- Biblioteka Nauki
Artykuł