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Finite size effects on the calorimetric cooperatity of the folding-unfolding transition in two-state proteins are considered using the Go lattice models with and without side chains. We show that for models without side chains a dimensionless measure of calorimetric cooperativity κ2 defined as the ratio of the van't Hoff to calorimetric enthalpy does not(More)
A number of experiments and experimentally based simulations showed that beta-proteins are mechanically more stable than alpha-proteins. However, the theory that might explain this evidence is still lacking. In this paper we have developed a simple elastic theory, which allows to estimate critical forces for stretching both kinds of proteins. It has been(More)
We analyze the dependence of thermal denaturation transition and folding rates of globular proteins on the number of amino acid residues, N. Using lattice Go models we show that ∆T /T F ∼ N −1 , where T F is the folding transition temperature and ∆T is the transition width computed using the temperature dependence of the order parameter that distinguishes(More)
Scaling of folding properties of proteins is studied in a toy system – the lattice Go model with various two-and three-dimensional geometries of the maximally compact native states. Characteristic folding times grow as power laws with the system size. The corresponding exponents are not universal. Scaling of the thermodynamic stability also indicates(More)
Since March 2009, the rapid spread of infection during the recent A/H1N1 swine flu pandemic has raised concerns of a far more dangerous outcome should this virus become resistant to current drug therapies. Currently oseltamivir (tamiflu) is intensively used for the treatment of influenza and is reported effective for 2009 A/H1N1 virus. However, as this(More)
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Finite size effects on the cooperative thermal denaturation of proteins are considered. A dimensionless measure of cooperativity, Omegac, scales as Nzeta, where N is the number of amino acids. Surprisingly, we find that zeta is universal with zeta=1+gamma, where the exponent gamma characterizes the divergence of the susceptibility for a self-avoiding walk.(More)
An accurate estimation of binding free energy of a ligand to receptor ΔG(bind) is one of the most important problems in drug design. The success of solution of this problem is expected to depend on force fields used for modeling a ligand-receptor complex. In this paper, we consider the impact of four main force fields, AMBER99SB, CHARMM27, GROMOS96 43a1,(More)
Using exhaustive Monte Carlo simulations we study the kinetics and mechanism of fibril formation using lattice models as a function of temperature (T) and the number of chains (M). While these models are, at best, caricatures of peptides, we show that a number of generic features thought to govern fibril assembly are captured by the toy model. The monomer,(More)