Life Sciences Commons^™

Effects Of The Microenvironment Surrounding Cys433 In Arabidopsis Β-Amylase-1 And -3 On The Sensitivity To Glutathionylation By Nitrosoglutathione, Matthew R. Kohler

Senior Honors Projects, 2010-2019

Glutathionylation is a reversible post-translational modification of proteins involving the transfer of glutathione to the thiols of specific cysteine residues. While the mechanism behind glutathionylation is known, the specificity of cysteine glutathionylation is not understood. It is known, however, that the two main factors affecting the susceptibility to glutathionylation are the reactivity and accessibility of cysteines in proteins, which is determined by the microenvironment. Using β-amylases (BAMs) 1 and 3 from Arabidopsis thaliana, which have different sensitivities to nitrosoglutathione (GSNO), as a model, I attempted to provide insight into why some cysteines are glutathionylated by GSNO and others are …

Protein, Methionine, And Cysteine Upregulation In Phaseolus Vulgaris ‘Black Turtle Bean’ Seeds Through Sulfur Fertilization At V2 And R2 Stages Of Growth, Hannah Paige Barry

Masters Theses

The purpose of this research was to increase protein, methionine, and cysteine content in Phaseolus vulgaris L., common bean in relation to the inhibitory compound tannin. Previous research has shown that sulfur fertilization increases total protein, methionine and cysteine content in various crops, but always in tandem with inhibitory compound increases. If successful, the resulting bean seed will have a better nutrient profile for malnourished populations around the world.

Granular gypsum was applied at 0 kg S ha^-1 [kilograms of sulfur per hectare], 10 kg S ha^-1, 20 kg S ha^-1, 40 kg S ha …