Please use this identifier to cite or link to this item:
|Title:||Rapid data collection for protein structure determination by NMR spectroscopy||Authors:||Xu, Y.
|Issue Date:||27-Jun-2007||Citation:||Xu, Y., Long, D., Yang, D. (2007-06-27). Rapid data collection for protein structure determination by NMR spectroscopy. Journal of the American Chemical Society 129 (25) : 7722-7723. ScholarBank@NUS Repository. https://doi.org/10.1021/ja071442e||Abstract:||A new approach is proposed to rapidly determine solution structures of small and medium-sized 13C,15N-labeled proteins, using a minimal number of experiments, such as 4D time-shared 13C/15N, 13C/15N-edited NOESY, 3D HNCA, and 3D MQ-(H)CCH-TOCSY. When the data are recorded on a 500 MHz spectrometer without using sparse sampling techniques, the experimental times were minimized to 2.5, 8.5, and 96 h for the HNCA, MQ-(H)CCH-TOCSY, and NOESY, respectively. The time-shared 4D NOESY contains four sub-spectra, one HC-NOESY-CH, one HC-NOESY-NH, one HN-NOESY-CH, and one HN-NOESY-NH. Sequence-specific assignment of backbone and side-chain resonances is achieved from the 3D spectra and the HC-NOESY-NH spectrum. Good initial structures can be quickly calculated using many unambiguous distance restraints that are easily obtained from the NOESY sub-spectra. The structures can be refined with more restraints assigned based on the initial structures. The approach has been demonstrated on ubiquitin (76 residues), liver fatty acid binding protein (129 residues, its NMR assignment and solution structure are presented here for the first time), and a cell-cell adhesion protein (214 residues). The approach will facilitate high throughput structure determination by NMR. Copyright © 2007 American Chemical Society.||Source Title:||Journal of the American Chemical Society||URI:||http://scholarbank.nus.edu.sg/handle/10635/101519||ISSN:||00027863||DOI:||10.1021/ja071442e|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.