A new twist on fluorescent labelling proteins

Incorporating a small fluorophore allows protein folding and redox states to be monitored

Labelling site for the atpt iodoacetamide structure

A new thiol-specific reagent can introduce a small bis(methylamino)terephthalic acid fluorophore into proteins. The noninvasive probe has distinct spectroscopic properties and can offer many advantages towards protein labelling, purification, and mechanistic work. Ekaterina Pletneva and her team at Dartmouth College in the US believe that this complex promises to serve as a powerful tool when it comes to studying protein folding and heme redox reactions.

 Did you find this result exciting? Then download the ChemComm communication to find out more. The article will be free to access until the 10th June 2011.

 

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