Molecular dynamics of PrP 180-193 has allowed us to investigate the stability of the alpha-helical conformation of the zwitterionic peptide (L-1) and the neutralized (L-2). In water, the helical structure of L-1 is unstable; in L-2, the alpha-helix breaks up in the middle at Gln186, and the two resulting connected helices are stable. The hydrophobic enviroment decreases the stability of the helical structure of L-1, this effect is more evident for L-2 for which the unfolding of the C-terminus is followed by the formation of an intramolecular hydrogen bond connecting His(187) with Thr(191). (C) 2004 Elsevier B.V. All rights reserved.

A molecular dynamics study on the conformational stability of PrP 180-193 helix II prion fragment

LA ROSA, Carmelo;Rizzarelli E;
2004-01-01

Abstract

Molecular dynamics of PrP 180-193 has allowed us to investigate the stability of the alpha-helical conformation of the zwitterionic peptide (L-1) and the neutralized (L-2). In water, the helical structure of L-1 is unstable; in L-2, the alpha-helix breaks up in the middle at Gln186, and the two resulting connected helices are stable. The hydrophobic enviroment decreases the stability of the helical structure of L-1, this effect is more evident for L-2 for which the unfolding of the C-terminus is followed by the formation of an intramolecular hydrogen bond connecting His(187) with Thr(191). (C) 2004 Elsevier B.V. All rights reserved.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.11769/40722
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