Josephine visited the LAB!
Matt Appell received for the Summer of 2018 the Helaine B. Allen Summer Fellowship! Congrats!
Yaotian Zhang received the Provost Summer Fellowship for 2018. Congrats!
04.27.2017
Jeremy G. Koob received his BS-MS degree in Biochemistry with Highest Honors (Christine Thomas/ Maria-Eirini Pandelia).
He is the recipient of the Nathan O. Kaplan Award! Congrats!
C&EN Global Enterprise , 2017, Vol.95(15), p.11-11
In a step toward understanding how the hepatitis B virus (HBV) replicates and causes infection, a research team has determined that one of the virus’s four proteins may incorporate a unique iron-sulfur cluster. Team leader Maria-Eirini Pandelia reported this discovery at the ACS meeting. The protein, known simply as X, is only 154 amino acids long and is the least understood of the HBV proteins. HBV infects the liver and can cause short-term and chronic illness. Biochemists know that X interacts with a number of proteins in host cells and that it plays a role in virus infectivity, replication, and ultimately cancer formation. However, the protein’s structure and mechanism have remained elusive. Pandelia’s team started investigating X last year, after work by another group indicated that the protein incorporates iron. Elemental and spectroscopic analysis by Pandelia and colleagues shows that the protein contains a [2Fe2S] cluster when isolated in the presence of oxygen. When reduced, the cluster converts to [4Fe4S]. Exactly how the conversion occurs is unclear. Research keeps revealing more about the diversity and importance of iron-sulfur clusters in biological chemistry, commented metalloprotein spectroscopist Joshua Telser of Roosevelt University. “It’s never-ending.”
Xingchen Liu received for the Summer of 2017 the Helaine B. Allen Summer Fellowship! Congrats!