The authors also make an effort to glean some mechanistic insight, but the inference that the channels are not passive and must change conformation requires the assumption that only a conformational change could underlie the intensity change, when in fact some sort of change upon binding might lead to a change in protonation without much of a conformational change.
Upon arrestin activation, several elements significantly change conformation, some becoming disordered in this state.
The drying process makes sedimentary organic matter change conformation, shrink in volume, and expose hydrophobic groups, thus becoming more hydrophobic.
Figure 4 maps known functional elements and arrestin switches (ASw, regions that significantly change conformation upon activation) on arrestin-3 structure.
Self-assembled branched DNA (bDNA) structures or DNA origami that change conformation in response to environmental cues hold great promises in sensing and actuation at the nanoscale.
Hammerhead ribozymes in crystals change conformation in response to deprotonation of the nucleophilic 2′ OH, thereby aligning the hydroxyl for in-line displacement at the scissile phosphate.
In this context we have designed pH-responsive, amphoteric polyamidoamines (PAAs) which change conformation on passing from a neutral pH (extracellular) to an acidic pH (endosomal and lysosomal) environments.
Studies show that GDSL hydrolases have a flexible active site that appears to change conformation with the presence and binding of the different substrates, much like the induced fit mechanism proposed by Koshland.
However, under an applied shear force, the persistence length of the polymer chain is assumed, through kinetic theories, to remain constant even though the polymer chain may change conformation.
We sought to facilitate the design of improved drug leads by defining residues most likely to change conformation, and then defining a minimal manifold of possible conformations of a target site for drug design based on a small number of identified flexible residues.
The biological function of proteins requires the ability to change conformation [17].
