Descrizione: Chemical ligation and protein semi? synthesis by expressed protein ligation (EPL) are powerful chemical tool to prepare selectively modified proteins with unnatural amino acids, post? translation modification, probes and stable isotope. In particular, EPL is based on the use of modified inteins, a class of protein which catalyze its self? splicing, to prepare recombinant thioester polypeptides which react chemoselectively with a synthetic peptide bearing a Cys residue at the N? terminal position to form an amide bond. We will apply this methodology for: -Semi-synthesis of double/triple labeled repeat protein for folding studies by single molecule FRET.-Segmental labeling of designed TPR proteins for folding studies by NMR.-Preparation of modified histone proteins H3 and H4 to understand the role of Histone modification in chromatin assembly.-Preparation of 13C and 15N labeled peptides
A synthetic strategy, based on expressed protein ligation, was developed to site-specific label TPR proteins with two different molecular probes
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119 Records (118 escludendo Abstract e Conferenze). Impact factor totale: 499.928 (497.078 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 504.208 (501.225 escludendo Abstract e Conferenze).