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