AI Article Synopsis
- The study provides almost complete resonance assignments for the oxidized form of the N-terminal domain of PilB from Neisseria meningitidis, focusing on the Cys(67)-Cys(70) structure.
- Secondary structure analysis was conducted using the CSI method and TALOS, predicting the presence of 7 alpha-helices and 5 beta-sheets in the protein.
- These findings contribute to the understanding of PilB's structure and potentially its function in this bacterium.
Article Abstract
We report the nearly complete 1H, 13C and 15N resonance assignments of the oxidized form (Cys(67)-Cys(70)) of the N-terminal domain of PilB from Neisseria meningitidis. Secondary structure determination using CSI method and TALOS leads mainly to the prediction of 7 alpha-helical and 5 beta-sheet parts.
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| http://dx.doi.org/10.1007/s12104-007-9038-8 | DOI Listing |
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