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.
• Języki publikacji: EN

Abstrakty

EN

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.

Słowa kluczowe

EN

peptide conformation; β-hairpin; hPin1 protein; NMR

PL

β-hairpin; hPin1 protein; NMR

• Wydawca: Politechnika Gdańska
• Czasopismo: TASK Quarterly : scientific bulletin of Academic Computer Centre in Gdansk
• Rocznik: 2014
• Tom: Vol. 18, No 4
• Strony: 343--349
• Opis fizyczny: Bibliogr. 14 poz., rys., wykr.

Twórcy

autor

Makowska J.

• Faculty of Chemistry, University of Gdansk Wita Stwosza 63, 80-308 Gdansk, Poland

autor

Uber D.

• Faculty of Chemistry, University of Gdansk Wita Stwosza 63, 80-308 Gdansk, Poland

autor

Żmudzińska W.

• Laboratory of Biopolymer Structure, Intercollegiate Faculty of Biotechology University of Gdansk–Medical University of Gdansk Kładki 24, 80-822 Gdansk, Poland

autor

Chmurzyński L.

• Faculty of Chemistry, University of Gdansk Wita Stwosza 63, 80-308 Gdansk, Poland

Bibliografia

• [1] Montelione G T, Scheraga H A 1989 Acc. Chem. Res. 22 70
• [2] Searle M S, Williams D H, Packman L C 1995 Nat. Struct. Biol. 2 999
• [3] Makowska J, Baginska K, Makowski M, Jagielska A, Liwo A, Kasprzykowski F, Chmurzynski L, Scheraga H A 2006 J. Phys. Chem. B 110 4451
• [4] Makowska J, Baginska K, Skwierawska A, Liwo A, Chmurzynski L, Schera ga H A 2008 Biopolymers 90 772
• [5] Makowska J, Uber D, Chmurzynski L 2012 J. Phys. Chem. B 116 653
• [6] Makowska J, Baginska K, Skwierawska A, Liwo A, Chmurzynski L, Schera ga H A 2008 Biopolymers 90 772
• [7] Plotnikov V, Rochalski A, Brandts M, Brandts J F, Williston S, Frasca V, Li n L N 2002 Assay Drug Dev. Technol. 1 83
• [8] Fasman G D 1996, Plenum Press, 738 66
• [9] Koradi R, Billeter M, Wuthrich K 1996 J. Mol. Graphics 14 51
• [10] Shamosand M I, Hoey D 1995, Closest-point problems of the 16th IEEE Symposium on the Foundations of Computer Science AQ6 151
• [11] Rohlf F J 1978 Information Process Lett. 7 44
• [12] Bentley J L, Friedman J H 1978 IEEE Trans. Comput. C-ZJ 97
• [13] Bentley J L, Weide B W, Yao A C 1980 ACM Trans. Math. Software 563
• [14] Greenfield N J 1996 Anal. Biochem. 235 1