Your assignment is to prepare and submit a paper on scientific challenges. It also frustrates functionally as well as structural studies (Martin et al 2005, p.1115).

Scientists as well as researchers do not understand how Hsp104, which is a hexameric AAA+ ATPase obtained from yeast, disaggregates various structures that include aggregates induced by stress, the prions and also the α-synuclein conformers are related with the Parkinson disease. The researcher aims in establishing the Hsp104 hexamers undergo various mechanisms of collaborating intersubunit to disaggregate the aggregates that are induced by stress versus the amyloid. So as to resolve the aggregates that are disordered the Hsp104 subunits team up in a non-cooperating manner by the employment of probabilistic substrate binding and also the ATP hydrolysis. The solutions to these problems enable humanity to understand the reverse function played by cells in amyloid formation (Barnhart & Chapman 2006, p. 140).

In making efforts to optimize and also reduce the side effects of therapy, the Hsp104 gets engineered and also potentiated to be able to dissolve specific aggregates. The aggregates should be related to Parkinson’s disease. The disaggregate activity of Hsp104can is tailored and also enhanced for any protein. Therefore, the Hsp104 variant that have been optimized by a substrate increases solubility of proteins. It also enhances the purification of proteins in various settings. Nevertheless, the limited understanding of the structure and mechanics of Hsp104 hexamers hinders the research. The individual subunits of the Hsp104 hexamer are not understood how they coordinate the translocation of substrates. It is also not understood how ATP hydrolysis solubilizes proteins that are unrelated and have been trapped in the aggregates (Martin et al 2005, p.1111).

The major question is how the single subunits work together to promote the remodeling of the substrate.&nbsp.