The representation of a proteinâ??s spatial sampling at atomic resolution is fundamental for understanding its function. NMR has been established as the best-suited technique toward this goal for small proteins. However, the accessible information content rapidly deteriorates with increasing protein size. We have recently demonstrated that for small proteins distance restraints with an accuracy smaller than 0.1Â*Ã? can be obtained by replacing traditional semi-quantitative Nuclear Overhauser Effects (NOEs) with exact NOEs (eNOE). The high quality of the data allowed us to calculate structural ensembles of the small model protein GB3 consisting of multiple rather than a single state. The analysis has been limited to small proteins because NOEs of spins with unresolved diagonal peaks cannot be used. Here we propose a simple approach to translate such NOEs into correct upper distance restraints, which opens access to larger biomolecules. We demonstrate that for 16Â*kDa cyclophilin A the collection of such restraints extends the original 1254 eNOEs to 3471.
[Stan NMR blog] NMR Data Evaluation: Review of Covariance Applications
NMR Data Evaluation: Review of Covariance Applications
Review of a novel NMR technique requiring special data evaluation.
Source: Stan blog library
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12-01-2014 12:17 PM
[Stan NMR blog] NMR Data Evaluation: Review of Covariance Applications
NMR Data Evaluation: Review of Covariance Applications
Review of an important new NMR technique requiring special data evaluation.
Source: Stan blog library
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02-11-2014 09:58 PM
[NMR paper] EZ-ASSIGN, a program for exhaustive NMR chemical shift assignments of large proteins from complete or incomplete triple-resonance data.
EZ-ASSIGN, a program for exhaustive NMR chemical shift assignments of large proteins from complete or incomplete triple-resonance data.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles EZ-ASSIGN, a program for exhaustive NMR chemical shift assignments of large proteins from complete or incomplete triple-resonance data.
J Biomol NMR. 2013 Sep 11;
Authors: Zuiderweg ER, Bagai I, Rossi P, Bertelsen EB
Abstract
For several of the proteins...
Evaluation of competing J domain:Hsp70 complex models in light of existing mutational and NMR data [Letters (Online Only)]
Evaluation of competing J domain:Hsp70 complex models in light of existing mutational and NMR data
Sousa, R., Jiang, J., Lafer, E. M., Hinck, A. P., Wang, L., Taylor, A. B., Maes, E. G....
Date: 2012-03-27
The work by Ahmad et al. (1) presented an NMR-based model for a bacterial DnaJ J domain:DnaK(Hsp70):ADP complex that differs from our crystal structure of a disulfide-linked bovine Hsc70:auxilin J domain complex (2). The work by Ahmad et al. (1) claimed that their model can better account for published mutational data, that their model is in better agreement with a previous NMR...
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03-27-2012 08:41 PM
Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins
Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins
Abstract In the last 15 years substantial advances have been made to place isotope labels in native and glycosylated proteins for NMR studies and structure determination. Key developments include segmental isotope labeling using Native Chemical Ligation, Expressed Protein Ligation and Protein Trans-Splicing. These advances are pushing the size limit of NMR spectroscopy further making larger proteins accessible for this technique. It is just emerging that segmental isotope...
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01-09-2011 12:46 PM
[NMR paper] 3D NMR experiments for measuring 15N relaxation data of large proteins: application t
3D NMR experiments for measuring 15N relaxation data of large proteins: application to the 44 kDa ectodomain of SIV gp41.
Related Articles 3D NMR experiments for measuring 15N relaxation data of large proteins: application to the 44 kDa ectodomain of SIV gp41.
J Magn Reson. 1998 Dec;135(2):368-72
Authors: Caffrey M, Kaufman J, Stahl SJ, Wingfield PT, Gronenborn AM, Clore GM
A suite of 3D NMR experiments for measuring 15N-¿1H¿ NOE, 15N T1, and 15N T1rho values in large proteins, uniformly labeled with 15N and 13C, is presented. These...
Extending the eNOE data set of large proteins by evaluation of NOEs with unresolved diagonals
Linear Mode
