Structure Calculation Using CS-RDC-ROSETTA: Difference between revisions
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== '''Introduction''' == | == '''Introduction''' == | ||
Conventional protein structure determination from NMR data relies heavily on complete or near complete side chain interproton distances. Obtaining such information can be both labor-intensive and time-consuming. CS-RDC-Rosetta (Ref. 1) is a new approach aimed at accurately determining protein structures up to 25 kDa using backbone chemical shifts, residual dipolar couplings and backbone amide proton | Conventional protein structure determination from NMR data relies heavily on complete or near complete side chain interproton distances. Obtaining such information can be both labor-intensive and time-consuming. CS-RDC-Rosetta (Ref. 1) is a new approach aimed at accurately determining protein structures up to 25 kDa by using backbone chemical shifts, residual dipolar couplings and backbone amide proton distances combined with the Rosetta protein structure modelling methodology, thereby circumventing the side chain assignment process. The sparse data serve to guide Rosetta conformational serach towards the lowest energy conformations in the folding landscape. | ||
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== '''Protocols''' == | == '''Protocols''' == | ||
Revision as of 21:28, 2 December 2009
Introduction
Conventional protein structure determination from NMR data relies heavily on complete or near complete side chain interproton distances. Obtaining such information can be both labor-intensive and time-consuming. CS-RDC-Rosetta (Ref. 1) is a new approach aimed at accurately determining protein structures up to 25 kDa by using backbone chemical shifts, residual dipolar couplings and backbone amide proton distances combined with the Rosetta protein structure modelling methodology, thereby circumventing the side chain assignment process. The sparse data serve to guide Rosetta conformational serach towards the lowest energy conformations in the folding landscape.
Protocols
The publication concerning the CS-RDC-Rosetta approach is currently under review. The protocols will be released upon publication.
References
1. Raman, S., Lange, O. et. al. (2009) Science, submitted.