Repozitorij Univerze v Novi Gorici

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Naslov:From polymers to proteins: the effect of side chains and broken symmetry on the formation of secondary structures within a Wang–Landau approach
Avtorji:Giacometti, Achille (Lastnik avtorskih pravic)
Datoteke:Gradivo nima datotek. Gradivo je morda fizično dosegljivo v knjižnici fakultete, zalogo lahko preverite v COBISS-u. Povezava se odpre v novem oknu
Jezik:Angleški jezik
Vrsta gradiva:Delo ni kategorizirano (r6)
Tipologija:1.01 - Izvirni znanstveni članek
Organizacija:UNG - Univerza v Novi Gorici
Opis:We use a micro-canonical Wang–Landau technique to study the equilibrium properties of a single flexible homopolymer where consecutive monomers are represented by impenetrable hard spherical beads tangential to each other, and non-consecutive monomers interact via a square-well potential. To mimic the characteristics of a protein-like system, the model is then refined in two different directions. Firstly, by allowing partial overlap between consecutive beads, we break the spherical symmetry and thus provide a severe constraint on the possible conformations of the chain. Alternatively, we introduce additional spherical beads at specific positions in the direction normal to the backbone, to represent the steric hindrance of the side chains in real proteins. Finally, we consider also a combination of these two ingredients. In all three systems, we obtain the full phase diagram in the temperature-interaction range plane and find the presence of helicoidal structures at low temperatures in the intermediate range of interactions. The effect of the range of the square-well attraction is highlighted, and shown to play a role similar to that found in simple liquids and polymers. Perspectives in terms of protein folding are finally discussed.
Ključne besede:Wang-Landau approach, Monte-Carlo simulations, proteins, secondary structures
Leto izida:2016
Št. strani:13
Številčenje:0
COBISS_ID:2954852  Povezava se odpre v novem oknu
URN:URN:SI:UNG:REP:X5Z2MTSO
DOI:10.1039/C6SM00542J Povezava se odpre v novem oknu
Število ogledov:2485
Število prenosov:0
Metapodatki:XML RDF-CHPDL DC-XML DC-RDF
Področja:Gradivo ni uvrščeno v področja.
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Skupna ocena:(0 glasov)
Vaša ocena:Ocenjevanje je dovoljeno samo prijavljenim uporabnikom.

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Gradivo je del revije

Naslov:Soft Matter
Založnik:Royal Society of Chemistry
ISSN:1744-683X
Leto izida:2016

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