Molecular dynamics of PrP 180-193 has allowed us to investigate the stability of the alpha-helical conformation of the zwittierionic peptide (L1) and the neutralized (L2). In water, the helical structure of L1 is unstable; in L2, the alpha-helix breaks up in the middle at Glnl86. and the two resulting connected helices are stable. The hydrophobic environment decreases the stability of the helical structure of L1, this effect is more evident for L2 for which the unfolding of the C-terminus is followed by the formation of an intramolecular hydrogen bond connecting His187 with Thr191.
M.PAPPALARDO, D.MILARDI, C.LA ROSA, C. ZANNONI, E.RIZZARELLI, D. GRASSO (2004). A Molecular Dynamics study on the conformational stability of 180-193 Prion second helix fragment. CHEMICAL PHYSICS LETTERS, 390, 511-516 [10.1016/j.cplett.2004.04.076].
A Molecular Dynamics study on the conformational stability of 180-193 Prion second helix fragment.
ZANNONI, CLAUDIO;
2004
Abstract
Molecular dynamics of PrP 180-193 has allowed us to investigate the stability of the alpha-helical conformation of the zwittierionic peptide (L1) and the neutralized (L2). In water, the helical structure of L1 is unstable; in L2, the alpha-helix breaks up in the middle at Glnl86. and the two resulting connected helices are stable. The hydrophobic environment decreases the stability of the helical structure of L1, this effect is more evident for L2 for which the unfolding of the C-terminus is followed by the formation of an intramolecular hydrogen bond connecting His187 with Thr191.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
