arXiv Β· Semantic Scholar Β· PubMed Β· Indexed academic papers
Enes, A, PiΓ±ero, A, Hermann, T, Zamanzadeh, A, Hennessy, T, Montenegro, D, Parnell, C, Jia, A, Weitzman, T, Wolf, M, Korakakis, PA, Swinton, PA, and Schoenfeld, BJ. How slow should you go? A systematic review with meta-analysis of the effect of resistance training repetition tempo on muscle hypertrophy. J Strength Coβ¦
We show that arguments in the comment by Schwab et al. quant-ph/0503018 on our recent work are invalid.β¦
This paper is a comment to M Wilkinson, EPL 106 (2014) 40001, arXiv:1401.4620 [physics.ao-ph,cond-mat.soft], which draws conclusion from our data that are at variance with our observations.β¦
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 computationally heavβ¦
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 Carlo studies of theβ¦
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 set of viable proteiβ¦
We discuss the problem of Poincare recurrences in area-preserving maps and the universality of their decay at long times. The work is related to to the results presented in Refs. [1,2].β¦
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 implemented in two body interaβ¦
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 $Ξ©_{c}$ resembling those seen in proteins arβ¦
The folding kinetics of a number of sequences for off-lattice continuum model of proteins is studied using Langevin simulations at two values of the friction coefficient. We show that there is a remarkable correlation between folding times, $Ο_{F}$, and $Ο= (T_{ΞΈ} - T_{F})/T_{ΞΈ} $, where $T_{ΞΈ}$ and $T_{F}$ are thβ¦