Structure Calculation Using CS-RDC-ROSETTA - Revision history

Jma at 23:16, 2 December 2009

2009-12-02T23:16:18Z

← Older revision		Revision as of 23:16, 2 December 2009
Line 3:		Line 3:
	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.		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.

	<br>		<br>

	== '''Protocols''' ==		== '''Protocols''' ==
Line 13:		Line 13:
	== '''References''' ==		== '''References''' ==

	1.    Raman, S., Lange, O. et. al. (2009) Science, submitted.		1.    Raman, S., Lange, O. et. al. (2009) ''Science'', submitted.

Jma at 21:28, 2 December 2009

2009-12-02T21:28:26Z

← Older revision		Revision as of 21:28, 2 December 2009
Line 1:		Line 1:
	== '''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 ~~distance~~, thereby circumventing the side chain assignment process.		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.

	<br>		<br>

	== '''Protocols''' ==		== '''Protocols''' ==

Jma: Created page with '== '''Introduction''' == Conventional protein structure determination from NMR data relies heavily on complete or near complete side chain interproton distances. Obtainin…'

2009-12-02T21:24:15Z

Created page with '== '''Introduction''' == Conventional protein structure determination from NMR data relies heavily on complete or near complete side chain interproton distances. Obtainin…'

New page

== '''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 distance, thereby circumventing the side chain assignment process.

<br>

== '''Protocols''' ==

The publication concerning the CS-RDC-Rosetta approach is currently under review.  The protocols will be released upon publication.

<br>

== '''References''' ==

1.    Raman, S., Lange, O. et. al. (2009) Science, submitted.