Sentence examples for rate of fold from inspiring English sources

Table 2 indicates that the improvement over SP3 and SP4 in success rate of fold recognition by SP5 exists in all three levels (family, superfamily, and fold).

There was a clear difference in the rate of fold increase between Ptc1Lox/Lox and Ptc1Lox/Lox NestinCre neocortical samples (clonal expansion of 0.7060±0.03302 vs. 0.8877±0.06774, p<0.05) (Fig. 2B) indicating that Hh pathway activation is mitogenic for cells that have a capacity to self-renew over an extended period of time.

The curvature elastic stress of synthetic phosphatidylcholine/phosphatidylethanolamine lipid bilayers can be used to control both the rate of folding and the yield of folded protein.

Addition of trifluoroethanol was found to accelerate the folding of the acylphosphatase variants, the extent of the acceleration being inversely proportional to the intrinsic rate of folding of the corresponding mutant.

By contrast, the doubly charged state shows a reduced rate of folding and a ϕ-value near 0.5 indicative of a repulsive interaction, and possibly also heterogeneity in the transition state ensemble.

That could slow the rate of translation and hence the rate of folding of the native protein.

Good agreement of the rate of folding when measured by tryptophan fluorescence emission and cold SDS PAGE implied a two-state folding mechanism [172].

Since LARS2 does not influence either the thermodynamic equilibrium between native and intermediate, or the rate of folding, it appears unlikely that the enzyme functions as a chaperone.

This is achieved by enhancing the rate of folding, protecting aggregation-prone intermediates from intermolecular interactions, or targeting misfolded proteins to the degradation machinery [208].

This will occur under conditions where the rate of folding is slow, a result of proteins that are specifically difficult to fold, or a result of the overall ER folding capacity being saturated.

We have studied a series of structural descriptors intended for describing protein shapes (the radius of gyration, the radius of cross-section, and the coefficient of compactness) and their possible connection with folding behavior, either rates of folding or the emergence of folding intermediates, and compared them with classical descriptors, protein chain length and contact order.