October 17, 2014
Co-Translational Folding Pattern of the Serpin, Alpha 1 AntiTrypsin
The Folding of serine protease inhibitor, specifically, the Alpha 1 Antitrypsin has been associated with forming aggregates in the endoplasmic reticulum (ER) that might lead to diseases like emphysema and bronchitis. During my summer research experience at the University of Massachusetts in the Department of Biochemistry and Molecular Biology, I had the opportunity examining folding pattern of the serpins (serine protease inhibitors) to be better able to investigate the causes of the diseases. Serpins are large, ~400 amino acid, proteins and thus are likely to begin folding co-translationally. We hypothesized that ribosome attached nascent chains in the ER lumen will search local folding energy minima in addition to with autonomous folding units (AFU) which can fold co-translationally.
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