Accurate protein structure modeling using sparse NMR data and homologous structure information
β Scribed by Thompson, J. M.; Sgourakis, N. G.; Liu, G.; Rossi, P.; Tang, Y.; Mills, J. L.; Szyperski, T.; Montelione, G. T.; Baker, D.
- Book ID
- 118201950
- Publisher
- National Academy of Sciences
- Year
- 2012
- Tongue
- English
- Weight
- 804 KB
- Volume
- 109
- Category
- Article
- ISSN
- 0027-8424
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract Routine structure prediction of new folds is still a challenging task for computational biology. The challenge is not only in the proper determination of overall fold but also in building models of acceptable resolution, useful for modeling the drug interactions and proteinβprotein comp
Acyl carrier proteins (ACPs) from spinach and from Escherichia coli have been used to demonstrate the utility of proton NMR for comparison of homologous structures. The structure of E. coli ACP had been previously determined and modeled as a rapid equilibrium among multiple conformational forms (Kim