Publications by authors named "Swechha Rimal"
Article Synopsis
- Folded proteins typically have a stable structure made of α-helices and β-sheets, but recent evidence from about 100 proteins suggests some can switch between these folds.
- A study predicts that 24% of sequences in the NusG transcription factor family may exhibit this fold-switching behavior, despite other methods not confirming this.
- Experimental validation through techniques like circular dichroism and NMR confirms the predictions for all tested variants, indicating that fold switching could be an important way of regulating gene expression across different life forms.
N-linked glycosylation is one type of posttranslational modification that proteins undergo during expression. The following describes the effects of N-linked glycosylation on high-level membrane protein expression in yeast with an emphasis on Saccharomyces cerevisiae. N-linked glycosylation is highlighted here as an important consideration when preparing membrane protein gene constructs for expression in S.
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