Zobrazeno 1 - 10
of 193
pro vyhledávání: '"Trovato, Antonio"'
Publikováno v:
Int. J. Mol. Sci. 21(1), 213 (2020)
Many native structures of proteins accomodate complex topological motifs such as knots, lassos, and other geometrical entanglements. How proteins can fold quickly even in the presence of such topological obstacles is a debated question in structural
Externí odkaz:
http://arxiv.org/abs/1911.08590
Publikováno v:
Scientific Reports (2019) 9:8426
Proteins must fold quickly to acquire their biologically functional three-dimensional native structures. Hence, these are mainly stabilized by local contacts, while intricate topologies such as knots are rare. Here, we reveal the existence of specifi
Externí odkaz:
http://arxiv.org/abs/1809.02173
Publikováno v:
J. Phys. A: Math. Theor. 50 (2017) 504001 (16pp)
The folding of a protein towards its native state is a rather complicated process. However there are empirical evidences that the folding time correlates with the contact order, a simple measure of the spatial organisation of the native state of the
Externí odkaz:
http://arxiv.org/abs/1709.01815
The presence of a thermodynamic phase of a three-stranded DNA, namely, a mixed phase of bubbles of two bound strands and a single one, is established for large dimensions ($d\geq 5$) by using exact real space renormalization group (RG) transformation
Externí odkaz:
http://arxiv.org/abs/1703.09432
Autor:
Amico, Tommaso, Dada, Samuel Toluwanimi, Lazzari, Andrea, Brezinova, Michaela, Trovato, Antonio, Vendruscolo, Michele, Fuxreiter, Monika, Maritan, Amos
Publikováno v:
eLife; 11/18/2024, p1-16, 16p
Autor:
Salicari, Leonardo1,2 (AUTHOR), Trovato, Antonio1,2 (AUTHOR) antonio.trovato@unipd.it
Publikováno v:
International Journal of Molecular Sciences. Jun2023, Vol. 24 Issue 11, p9193. 16p.
Publikováno v:
Scientific Reports 6, 33872 (2016)
The presence of knots has been observed in a small fraction of single-domain proteins and related to their thermodynamic and kinetic properties. The exchanging of identical structural elements, typical of domain-swapped proteins, make such dimers sui
Externí odkaz:
http://arxiv.org/abs/1607.01414
Autor:
Mullick, Pratik1,2,3 (AUTHOR), Trovato, Antonio1,4 (AUTHOR) antonio.trovato@unipd.it
Publikováno v:
Biomolecules (2218-273X). Dec2022, Vol. 12 Issue 12, p1771. 21p.
Publikováno v:
Phys. Rev. E 89, 012121 (2014)
Thermal denaturation of DNA is often studied with coarse-grained models in which native sequential base pairing is mimicked by the existence of attractive interactions only between monomers at the same position along strands (Poland and Scheraga mode
Externí odkaz:
http://arxiv.org/abs/1306.4206
We argue that protein native state structures reside in a novel "phase" of matter which confers on proteins their many amazing characteristics. This phase arises from the common features of all globular proteins and is characterized by a sequence-ind
Externí odkaz:
http://arxiv.org/abs/1204.2725