Samuely et al. (cond-mat/0503153) make the strong claim that our letter is 'contradicting several established experimental results'. As we will show below this is not justified and the claims from are based on a misinterpretation of our results.…
We comment on various incorrect claims made in a recent paper by Grosu et al. (cond-mat/0101392).…
Reply to the recent comment by I.Ispolatov and M.Karttunen, cond-mat/0303564…
The work of our group on reproducing scenarios of high energy theoretical physics on Dirac materials, like graphene, is illustrated. The main goal of this paper is to explain how versatile these systems are, and how far and wide into the hep-th territory we can explore with them. I first review why …
This submission is a duplicate of cond-mat/0608646.…
Background: Many attempts have been made to resolve in time the folding of model proteins in computer simulations. Different computational approaches have emerged. Some of these approaches suffer from the insensitivity to the geometrical properties of the proteins (lattice models), while others are …
We demonstrate that the recently proposed pruned-enriched Rosenbluth method PERM (P.~Grassberger, Phys.~Rev.~{\bf E 56} (1997) 3682) leads to very efficient algorithms for the folding of simple model proteins. We test it on several models for lattice heteropolymers, and compare to published Monte …
We discuss recent theoretical developments in the study of simple lattice models of proteins. Such models are designed to understand general features of protein structures and mechanism of folding. Among the topics covered are (i) the use of lattice models to understand the selection of the limited …
Different aspects of protein folding are illustrated by simplified polymer models. Stressing the diversity of side chains (residues) leads one to view folding as the freezing transition of an heteropolymer. Technically, the most common approach to diversity is randomness, which is usually implemente…
We consider equilibrium folding transitions in lattice protein models with and without side chains. A dimensionless measure, $Omega_{c}$, is introduced to quantitatively assess the degree of cooperativity in lattice models and in real proteins. We show that larger values of $Ω_{c}$ resembling those…