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Unfolding force

Rief, M., Pascual, J., Saraste, M., and Gaub, H. E. (1999). Single molecule force spectroscopy of spectrin repeats Low unfolding forces in helix bundles. J. Mol. Biol. 286, 553-561. [Pg.243]

Figure 10-11. Unfolding forces of secondary structural elements depend on temperature. (A) Rupture forces of main peaks, which exhibited no side peaks... Figure 10-11. Unfolding forces of secondary structural elements depend on temperature. (A) Rupture forces of main peaks, which exhibited no side peaks...
Fig. 17.7. Engineered protein designed for mechanochemistry studies, (a) A pair of cysteine residues introduced into the 127 protein (positions 32 and 75 suifur atoms as spheres) spontaneously form a buried disuifide bond. (b). In response to an unfolding force, the protein extends right up to the disuifide bond. Unfoiding exposes the disulfide bond to the solution, (c) Then, a nucieophiie such as DTT can initiate a Sn2 reaction, leading to the reduction of the disuifide bond and the concomitant extension of the amino acids that were trapped behind the disuifide bond. This sequence of events nnambiguousiy identifies individual disulfide bond reduction events, allowing for the stndy of a pulling force on a Sn2 chemicai reaction... Fig. 17.7. Engineered protein designed for mechanochemistry studies, (a) A pair of cysteine residues introduced into the 127 protein (positions 32 and 75 suifur atoms as spheres) spontaneously form a buried disuifide bond. (b). In response to an unfolding force, the protein extends right up to the disuifide bond. Unfoiding exposes the disulfide bond to the solution, (c) Then, a nucieophiie such as DTT can initiate a Sn2 reaction, leading to the reduction of the disuifide bond and the concomitant extension of the amino acids that were trapped behind the disuifide bond. This sequence of events nnambiguousiy identifies individual disulfide bond reduction events, allowing for the stndy of a pulling force on a Sn2 chemicai reaction...
Under dynamic conditions, the refolding force, F p, is lower than the unfolding force under steady-state as well as dynamic conditions [45]. [Pg.348]

It has been found that the lifetime of an adhesin is rather long (>ls) for forces below the steady-state unfolding force, [48]. This implies that it... [Pg.350]

In elongation region II, the force to which the adhesin is exposed is equal to the unfolding force, Fu up- This implies that the bond opening rate for the adhesin, kj F), can, for the two cases with slow or fast elongation (i.e., for L < L and L > L, respectively), be written as... [Pg.350]

The reported unfolding force of type 1 pilus by Miller et al. [50] of 60 pN was performed for an elongation speed of l-3 xm/s. Since this is significantly higher than the corner frequency, L, their value is assumed to be an assessment of the unfolding force under dynamic conditions. [Pg.355]

Here, we report on single-molecule stretching of native fibronectin and the influence of the compatible solutes ectoine and sarcosine on the mechanical properties, as revealed by the unfolding of the individual subunits and the overall persistence length of the macromolecule [131], In accordance with the preferential exclusion model, we found a significant stabilization of the protein structure in the presence of osmolytes but not an increase in unfolding forces. [Pg.35]

Fig. 28 Unfolding force of FN-in domains as a function of domain number and presence of ectoine. Reproduced from [131] by permission of the PCCP Owner Societies... Fig. 28 Unfolding force of FN-in domains as a function of domain number and presence of ectoine. Reproduced from [131] by permission of the PCCP Owner Societies...
For eYFP, Fernandez and coworkers determined an unfolding force of approx. 60 pN. As the fluorescence is closely linked to the native state of the protein, mechanical unfolding switches its fluorescence off. ... [Pg.401]


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See also in sourсe #XX -- [ Pg.347 , Pg.348 , Pg.350 , Pg.351 , Pg.352 , Pg.355 , Pg.357 ]




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