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Thus, proteins that are found as conformational ensembles may have more than one functional conformation and multiple functions.
These proteins are referred to as chaperones or stress proteins because they exhibit a critical function in assisting newly synthesized polypeptides (clients) in achieving functional conformation, localization, activation and oligomerization.
Yagi, H. et al. Functional conformation changes in the F1-ATPase β subunit probed by 12 tyrosine residues.
The studies demonstrate that functional conformation and stability are largely governed by ionic interactions and active site disulfide plays a vital role in maintaining functional conformation.
The study of GAL4-Myb fusions suggests that this region is important in maintaining a fully functional conformation of v-Myb.
MCS gaps could be reduced, from 20 30 nm to within 5 15 nm, to provide a functional conformation highly amenable to Ca2+ exchange (Phillips and Voeltz, 2016).
This result indicates that the refolded recombinant protein is in a functional conformation.
We suggest that the overwound right-handed RadA filament represents a functional conformation in the homology search and pairing reaction.
Chaperones are group proteins (i.e. heat shock proteins) that assist and protect intracellular proteins during cell life to maintain their functional conformation [65].
Thus, the CTD of the mycobacterial CoaE might also act in a similar fashion and thereby assist the NTD in attaining its biologically functional conformation.
These results together, raise the possibility that the 61 right-handed helical filaments may not be the only functional conformation for RecA family proteins.
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