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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 …
Studies Into The Structure And Function Of Various Domains Of Obscurin And Titin, Rachel A. Policke
Studies Into The Structure And Function Of Various Domains Of Obscurin And Titin, Rachel A. Policke
Senior Honors Projects, 2010-2019
Muscles give our bodies the ability to move by stretching and contracting. While contraction is accomplished by the well-known actin-myosin interaction, not much is known about stretch. Two integral muscle proteins involved in stretch are titin and obscurin; both are long rope-like protein molecules that seem to act as molecular springs. Mutations in these two proteins can lead to diseases such as hypertrophic cardiomyopathy and muscular dystrophy, as well as a variety of cancers. In an effort to understand muscle stretch and signaling on a more fundamental level, here we present the high resolution structure of obscurin Ig59, a domain …