Thursday, February 8, 2018

Back in the swing

Today, since we finished all the presentations, I went back to working on my thesis.

the feedback that I got for my presentation was helpful, and I'll use it for next time.

So, today I took a closer look at the quaternary structure of the proteins (in aqueous solution anyway). Apparently it doesn't have any "considerable" secondary or tertiary structure. "Particularly in their repetitive core domains, however, the long repetitive sequences permit weak but numerous intra- and intermolecular interactions between neighboring domains and proteins upon passage through the spinning duct." And it's because of these interactions through the extrusion, that the secondary through tertiary structures emerge as the proteins polymerize.

Cool stuff.

Also, "the high electron density regions comprise crystalline sub-structures with high β-sheet content. These sub-structures are thought to be responsible for the mechanical strength of the silk thread. The elasticity of silk is based on the areas with low electron density, which are characterized by amorphous structures with few defined elements of secondary or supersecondary structure.40, Such arrangement closely resembles that of protein hydrogels. Upon tensile loading, the hydrogel-like areas can partially deform, contributing to the elasticity and flexibility of the thread." 

This gives me a better understanding of the chemical/physical reasons for the rigidity/elasticity.

I'm really enjoying this topic, and I can't wait to present my finished project! I should probably start that paper soon...

All in a day's work,

- Noah

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