Sandi Brudar (Avtor), Barbara Hribar (Avtor)

Povzetek

The aggregation of human $\gamma$-D crystallin is associated with the age-onset cataract formation. Here, we extensively investigated the self-association mechanism of human $\gamma$-D crystallin through molecular dynamics computer simulations. By mutating the protein surface we found that electrostatic interactions between charged amino acids play a crucial role in its self-association. We have confirmed the two-fold role of arginine molecules. If they are located as residues on the protein surface they can initiate protein contacts and contribute to their stickiness with noteworthy hydrophobic interactions through stacking of their methylene groups. But if they are added as free arginine in the protein solution they can also stabilize it, by associating with the protein surface and also with themselves to form effective inter-protein spacers that obstruct protein aggregation.

Ključne besede

gama-D-kristalin;samozdruževanje;arginin;simulacija molekulske dinamike;gamma-D-crystallin;self-assembly;arginine;MD simulation;

Podatki

Jezik: Angleški jezik
Leto izida:
Tipologija: 1.01 - Izvirni znanstveni članek
Organizacija: UL FKKT - Fakulteta za kemijo in kemijsko tehnologijo
UDK: 577.322
COBISS: 157958915 Povezava se bo odprla v novem oknu
ISSN: 0167-7322
Št. ogledov: 263
Št. prenosov: 25
Ocena: 0 (0 glasov)
Metapodatki: JSON JSON-RDF JSON-LD TURTLE N-TRIPLES XML RDFA MICRODATA DC-XML DC-RDF RDF

Ostali podatki

Sekundarni jezik: Slovenski jezik
Sekundarne ključne besede: gama-D-kristalin;samozdruževanje;arginin;simulacija molekulske dinamike;
Vrsta dela (COBISS): Članek v reviji
Strani: str. 1-8
Zvezek: ǂVol. ǂ386, [article no.] 122461
Čas izdaje: 15 Sep. 2023
DOI: 10.1016/j.molliq.2023.122461
ID: 19766060