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Full-Text Articles in Life Sciences

A Nosy Neighbor: Purification And Functional Characterization Of Lpg2149, Ashley M. Holahan Oct 2021

A Nosy Neighbor: Purification And Functional Characterization Of Lpg2149, Ashley M. Holahan

The Journal of Purdue Undergraduate Research

Ubiquitination is a process that marks proteins for various cell-signaling pathways, namely protein degradation and other processes. Th ese pathways are essential in a wide array of cellular processes, including defense mechanisms against invading pathogens. Th e ubiquitination process is universally found in all eukaryotic organisms, including plants and animals, and thus plays a vital role in cellular homeostasis. Recently, more discoveries have been made on prokaryotic effector proteins that hijack the ubiquitination system even when they do not possess a ubiquitin system of their own. MavC, also known as lpg2147 (Gan, Nakayasu, Hollenbeck, & Luo, 2019; Puvar et al., …


Structural And Functional Characterization Of Hyper-Phosphorylated Grk5 Protein Expressed From E. Coli, Joseph M. Krampen, John Tesmer, Qiuyan Chen Aug 2018

Structural And Functional Characterization Of Hyper-Phosphorylated Grk5 Protein Expressed From E. Coli, Joseph M. Krampen, John Tesmer, Qiuyan Chen

The Summer Undergraduate Research Fellowship (SURF) Symposium

G protein-coupled receptor (GPCR) kinases (GRKs) are proteins in the cell responsible for regulating GPCRs located on the cell membrane. GRKs regulate active GPCRs by phosphorylating them at certain sites which causes them to stop normal signaling on the membrane. This ultimately affects how the cell responds to its environment. GRK5 is a kinase of particular interest due to its involvement in the pathology of diseases such as cardiac failure, cancers, and diabetes. Understanding the structure and function of GRK5 is essential for discovering ways to manipulate its behavior with these diseases, but not much is known about how GRK5 …


Determining The Structure Of Phospholipase C Epsilon, Hannah O'Neill, Monita Sieng, Elisabeth Garland-Kuntz, Angeline Lyon Aug 2017

Determining The Structure Of Phospholipase C Epsilon, Hannah O'Neill, Monita Sieng, Elisabeth Garland-Kuntz, Angeline Lyon

The Summer Undergraduate Research Fellowship (SURF) Symposium

The phospholipase C (PLC) epsilon subfamily of PLC enzymes are found at highest concentration within the cardiovascular system. Improper functioning of the enzyme, whether due to overstimulation or changes in expression, has far-reaching effects within the human body Stunted heart valve development and cardiac hypertrophy and are two such examples. The mechanisms by which PLC epsilon activity is regulated in these processes remain unknown, as does the physical structure of the enzyme. In this study, we seek to determine the structure of a PLC epsilon fragment that retains enzymatic activity and is amenable to crystallization. Mutagenesis of PLC epsilon cDNA …


Structural Studies On The Rubella Virus Capsid Protein And Its Organization In The Virion, Vidya Mangala Prasad Oct 2013

Structural Studies On The Rubella Virus Capsid Protein And Its Organization In The Virion, Vidya Mangala Prasad

Open Access Dissertations

Rubella virus is a leading cause of birth defects due to infectious agents. When contracted during pregnancy, rubella infection leads to severe damage in fetuses. Despite its medical importance, very little is known about the structure of the pleomorphic rubella virus as compared to its alphavirus relatives. The rubella capsid protein is a critical structural component of virions as well as a key factor in virus-host interactions. Three crystal structures of the structural domain of the rubella capsid protein have been described here. The polypeptide fold of the capsid protomer has not been observed previously. The capsid protein structure, along …