1H, 13C and 15N NMR backbone assignments of the 269-residue serine protease PB92 from Bacillus alcalophilus |
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Authors: | Rasmus H Fogh Dick Schipper Rolf Boelens Robert Kaptein |
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Institution: | (1) Department of Chemistry, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands;(2) Gist-Brocades B.V., Research and Development, P.O. Box 1, 2600 MA Delft, The Netherlands |
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Abstract: | Summary The 1H, 13C and 15N 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.Abbreviations 2D/3D
two-/three-dimensional
- HSQC
Heteronuclear Single Quantum Coherence
- TOCSY
total correlation spectroscopy
- NOE
nuclear Overhauser effect
Supplementary material available from the authors: One table containing the backbone 15N, 1HN, 13CO , 13CO and 1H assignments for serine protease PB92. |
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Keywords: | Triple-resonance spectroscopy NMR spectrum assignment Secondary structure |
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