Photo-CIDNP study of interactions of serine proteinases with their protein inhibitors

✍ Scribed by K. A. Muszkat; S. Weinstein; I. Khait; M. Vered

• Book ID: 101719596
• Publisher: Wiley (John Wiley & Sons)
• Year: 1983
• Tongue: English
• Weight: 247 KB
• Volume: 22
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.360220150

✦ Synopsis

Israel

Synopsis

Photochemically induced dynamic nuclear polarization was used to study the accessibility of surface tyrosine and tryptophan residues in proteinases, in their protein inhibitors and in the proteinase-inhibitor complexes. The accessibility probe is the triplet of 10-(carboxyethyl) flavin formed by optical excitation. On complex formation we observe accessibility loss in the surface tyrosines and tryptophans in the proximity of the proteinase-inhibitor contact site, and in the case of bovine pancreatic trypsin inhibitor, in more distant tyrosines as well.