Measles
Study data from V. Belle et al provide new insights into measles
Published in Medical Imaging Law Weekly, January 27th, 2009
"Using site-directed spin-labeling EPR spectroscopy, we mapped the region of the intrinsically disordered C-terminal domain of measles virus nucleoprotein (N-TAIL) that undergoes induced folding. In addition to four spin-labeled N-TAIL variants (S407C, S488C, L496C, and V517C) (Morin et al. (2006), J Phys Chem 110: 2059620608), 10 new single-site cysteine variants were designed, purified from E. coli, and spin-labeled," scientists writing in the journal Proteins - Structure Function and Bioinformatics report.
"These 14 spin-labeled variants enabled us to map in detail the gain of rigidity of N-TAIL in the presence of either the secondary structure stabilizer...
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