Naslov
Hydrogen Bond Networks and Hydrophobic Effects in the Amyloid β30–35 Chain in Water: A Molecular Dynamics Study

Autori
Jong, KwangHyok ; Grisanti, Luca ; Hassanali, Ali

Izvornik
Journal of Chemical Information and Modeling (1549-9596) 57 (2017), 7; 1548-1562

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
hydrogen bonds ; oligopeptides

Sažetak
We have studied the conformational landscape of the C-terminal fragment of the amyloid protein Aβ30–35 in water using well-tempered metadynamics simulations and found that it resembles an intrinsically disordered protein. The conformational fluctuations of the protein are facilitated by a collective reorganization of both protein and water hydrogen bond networks, combined with electrostatic interactions between termini as well as hydrophobic interactions of the side chains. The stabilization of hydrophobic interactions in one of the conformers involves a collective collapse of the side chains along with a squeeze-out of water sandwiched between them. The charged N- and C-termini play a critical role in stabilizing different types of protein conformations, including those involving contact-ion salt bridges as well as solvent-mediated interactions of the termini and the amide backbone. We have examined this by probing the distribution of directed water wires forming the hydrogen bond network enveloping the polypeptide. Water wires and their fluctuations form an integral part of structural signature of the protein conformation.

Izvorni jezik
Engleski

Znanstvena područja
Fizika, Kemija

POVEZANOST RADA