Repozitorij Univerze v Novi Gorici

Izpis gradiva
A+ | A- | Pomoč | SLO | ENG

Naslov:Entropic cost of folding and phase diagrams of polypeptides: Why are IDPs unfolded at room temperature?
Avtorji:ID Badasyan, Artem, Univerza v Novi Gorici (Avtor)
Datoteke: Gradivo nima datotek, ki so prostodostopne za javnost. 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
Tipologija:3.14 - Predavanje na tuji univerzi
Organizacija:UNG - Univerza v Novi Gorici
Opis:In spin models, that are applied to describe the conformational transitions in polymers, the number of spin orientations, that correspond to the disordered conformation, can be estimated using fundamental definitions of Statistical Physics. For instance, when considering alpha-helix to coil transition in polypeptides, the role of generalized coordinates is played by pairs of torsional angle, and the repeating unit populates different regions of that 2D contour map, depending on conformation. By scanning over all possible torsional angles, that do not violate the obvious limitations due to the excluded volume, the so-called Ramachandran map can be plotted, which is actually the phase space visualization for the helix-coil transition problem. The region of phase space, corresponding to the ordered, helical conformations, is much more limited, than the one, corresponding to all other (allowed) conformations. We can calculate the areas of these regions as Γhelix and Γcoil , and construct the ratio Q = Γcoil . Naturally, it can be interpreted as log(Q) = Scoil − Shelix = ΔS, the entropic cost of helix with respect to coil. To illustrate the importance of the entropic price of ordered conformation we report our recent results, that allowed to explain the peculiarity of phase diagrams of Intrinsically Disordered Proteins (IDP) out of larger Q-values, as compared to globular counterparts. In particular, it has been shown, that due to larger Q, the phase diagram of IDP is shifted towards higher temperatures.
Ključne besede:IDP, protein folding, phase diagram
Kraj izvedbe:Dept. of Physics, Free University of Berlin, Arnimallee 14 14195 Berlin, Germany
Leto izvedbe:2016
PID:20.500.12556/RUNG-2460 Novo okno
COBISS.SI-ID:4407291 Novo okno
NUK URN:URN:SI:UNG:REP:NZVCQ2J3
Datum objave v RUNG:23.06.2016
Število ogledov:4573
Število prenosov:0
Metapodatki:XML RDF-CHPDL DC-XML DC-RDF
:
Kopiraj citat
  
Skupna ocena:(0 glasov)
Vaša ocena:Ocenjevanje je dovoljeno samo prijavljenim uporabnikom.
Objavi na:Bookmark and Share


Postavite miškin kazalec na naslov za izpis povzetka. Klik na naslov izpiše podrobnosti ali sproži prenos.

Nazaj