Abstract
A family of Clostridium perfringens glycoside hydrolases (CpGH84A-E), with a conserved family 84 catalytic module, are thought to target the gastric mucosal layer. Chemical shift assignments have been completed for a putative protein-protein interaction X82 module from CpGH84C.
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Acknowledgements
We acknowledge Dr. Ryan MacKay at NANUC (University of Alberta) for data collection on the 800 MHz spectrometer and technical support. This work was supported by CIHR operating grants to S.P.S. (MOP-77776) and A.B.B. (MOP-68913). S.C. is the recipient of a Franklin Bracken Doctoral Scholarship. E.B. is a NSERC Doctoral Fellowship and a Michael Smith Foundation for Health Research Doctoral Fellowship awardee, J.J.A. is supported by a NSERC Doctoral Fellowship. K.G. is a University of Victoria Graduate Fellowship awardee. A.B.B. is a Canada Research Chair in Molecular Interactions and S.P.S. is a Canadian Institutes of Health Research New Investigator.
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Chitayat, S., Ficko-Blean, E., Adams, J.J. et al. NMR assignment of backbone and side chain resonances for a putative protein–protein interaction module from a family 84 glycoside hydrolase of Clostridium perfringens . Biomol NMR Assign 1, 7–9 (2007). https://doi.org/10.1007/s12104-007-9001-8
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DOI: https://doi.org/10.1007/s12104-007-9001-8