1H, 13C and 15N NMR backbone assignments of the 269-residue serine protease PB92 from Bacillus alcalophilus

Rasmus H. Fogh; Dick Schipper; Rolf Boelens; Robert Kaptein

doi:10.1007/BF00178340

¹H, ¹³C and ¹⁵N NMR backbone assignments of the 269-residue serine protease PB92 from Bacillus alcalophilus

Rasmus H. Fogh^*, Dick Schipper, Rolf Boelens, Robert Kaptein

^*Corresponding author for this work

Sub NMR Spectroscopy

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

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.

Original language	English
Pages (from-to)	123-128
Number of pages	6
Journal	Journal of Biomolecular NMR
Volume	4
Issue number	1
DOIs	https://doi.org/10.1007/BF00178340
Publication status	Published - Jan 1994

Keywords

NMR spectrum assignment
Secondary structure
Triple-resonance spectroscopy

Access to Document

10.1007/BF00178340

Cite this

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title = "1H, 13C and 15N NMR backbone assignments of the 269-residue serine protease PB92 from Bacillus alcalophilus",

abstract = "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.",

keywords = "NMR spectrum assignment, Secondary structure, Triple-resonance spectroscopy",

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AU - Schipper, Dick

AU - Boelens, Rolf

AU - Kaptein, Robert

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AB - 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.

KW - NMR spectrum assignment

KW - Secondary structure

KW - Triple-resonance spectroscopy

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