Abstract
One of the small proteins from Helicobacter pylori, acyl carrier protein (ACP), was investigated by NMR. ACP is related to various cellular processes, especially with the biosynthesis of fatty acid. The basic NMR resonance assignment is a prerequisite for the validation of a heterologuous protein interaction with ACP in H.pylori. Here, the results of the backbone 1H, 15N, and 13C resonance assignments of the H. pylori ACP are reported using double- and triple-resonance techniques. About 97% of all of the 1HN, 15N, 13CO, 13Cα, and 13Cβ resonances that cover 76 of the 78 non-proline residues are clarified through sequential- and specific- assignments. In addition, four helical regions were clearly identified on the basis of the resonance assignments.
Original language | English |
---|---|
Pages (from-to) | 505-507 |
Number of pages | 3 |
Journal | Journal of Biochemistry and Molecular Biology |
Volume | 36 |
Issue number | 5 |
DOIs | |
State | Published - 30 Sep 2003 |
Keywords
- ACP
- H. pylori
- NMR