Sentence examples for fold free from inspiring English sources

Additionally, this level of DSB formation is 1.5 fold (nucleosomal-bound DNA) and 1.2 fold (free DNA) lower than that seen with the AP/AP − 3 cluster, reflecting the reduction in the efficiency of AP site incision on strand 2 in the AP/AP + 1 cluster.

This stems from the sigmoidal relation between the fraction of folded proteins and folding free energy (eq. 1) (Chen and Shakhnovich 2009).

Computational studies have reported that miRNA precursor sequences have significantly higher negative minimal folding free energies (MFEs) and minimal folding free energy indexes (MFEIs) than other non-coding RNAs or mRNAs [ 60].

The POPMuSiC algorithm was applied to predict the folding free energy change (ΔDG) of amino acid substitution.

Using (R -selective amine tR -selectivefrom aminegillus transaminaseATA) as a transaminase model, in silico design was applied employing B-fromor Aspergillus free energy (ΔΔGfold) calculaterreus

These have been successfully applied to molecular dynamics simulations, the scoring of protein conformations, and the calculation of binding affinities and folding free energy landscapes.

Recent advances in computational protein design have allowed exciting new insights into the sequence dependence of protein folding free energy landscapes.

The Vfold-predicted loop entropies (Table 2) enable folding free energy calculations for RNA/RNA complex such as for microRNA target-binding (Cao and Chen 2012) and hairpin–hairpin kissing comicroRNA target-bindingCaon 2011; Candet al. 2014).

In order to improve the thermostability of feruloyl esterase A (FaeA) from Aspergillus niger CIB 423.1, the PoPMuSiC algorithm was applied to predict the folding free energy change (ΔΔG) of amino acid substitutions.

PoPMuSiC, a program that uses database-derived mean force potentials to predict changes in folding free energy resulting from single-site mutations, was used to modulate rationally the polymerization propensity of α1-antitrypsin.

Mutation sites were selected by targeting flexible regions with the greatest B-factors, and were substituted with amino acids that were determined by folding free energy calculations (ΔΔGfold < 0) to be more rigid than the original ones.