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Backbone1H,13C,15N NMR assignments of the unliganded and substrate ternary complex forms of mevalonate diphosphate decarboxylase fromStreptococcus pneumoniae

โœ Scribed by Guido Reuther; Richard Harris; Mark Girvin; Thomas S. Leyh

Book ID
107599587
Publisher
Springer-Verlag
Year
2010
Tongue
English
Weight
449 KB
Volume
5
Category
Article
ISSN
1874-2718

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1H,13C and15N NMR backbone assignments o
1H,13C and15N NMR backbone assignments of the 269-residue serine protease PB92 fromBacillus alcalophilus
โœ Rasmus H. Fogh; Dick Schipper; Rolf Boelens; Robert Kaptein ๐Ÿ“‚ Article ๐Ÿ“… 1994 ๐Ÿ› Springer Netherlands ๐ŸŒ English โš– 315 KB

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.