1H,13C and15N NMR backbone assignments of the 269-residue serine protease PB92 fromBacillus alcalophilus

✍ Scribed by Rasmus H. Fogh; Dick Schipper; Rolf Boelens; Robert Kaptein

• Publisher: Springer Netherlands
• Year: 1994
• Tongue: English
• Weight: 315 KB
• Volume: 4
• Category: Article
• ISSN: 0925-2738
• DOI: 10.1007/bf00178340

✦ Synopsis

The IH, 13C and ~SN NMR resonances of the backbone of serine protease PB92 have been assigned. This 269-residue protein is one of the largest monomeric proteins assigned so far. The amount and quality of information available suggest that even larger proteins could be assigned with present methods. Measured chemical shifts show excellent agreement with the secondary structure.

The constant improvement of NMR techniques (for a review, see Bax and Grzesiek, 1993) has permitted the assignment of the NMR spectra of ever larger proteins (e.g.