Publication date: 3 February 2015 Source:Structure, Volume 23, Issue 2
Author(s): Martin Billeter
The precision of an NMR structure may be manipulated by calculation parameters such as calibration factors. Its accuracy is, however, a different issue. In this issue of Structure, Buchner and Güntert present “consensus structure bundles,” where precision analysis allows estimation of accuracy.
[NMR paper] Three-dimensional structure and mimetic-membrane association of consensus 11-amino-acid motif from soybean lea3 protein.
Three-dimensional structure and mimetic-membrane association of consensus 11-amino-acid motif from soybean lea3 protein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Three-dimensional structure and mimetic-membrane association of consensus 11-amino-acid motif from soybean lea3 protein.
Biopolymers. 2012;98(1):59-66
Authors: Xue R, Liu Y, Zheng Y, Wu Y, Li X, Pei F, Ni J
Abstract
The occurrence of a highly conserved 11-mer repeating...
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VITAL NMR: using chemical shift derived secondary structure information for a limited set of amino acids to assess homology model accuracy
VITAL NMR: using chemical shift derived secondary structure information for a limited set of amino acids to assess homology model accuracy
Abstract Homology modeling is a powerful tool for predicting protein structures, whose success depends on obtaining a reasonable alignment between a given structural template and the protein sequence being analyzed. In order to leverage greater predictive power for proteins with few structural templates, we have developed a method to rank homology models based upon their compliance to secondary structure derived from experimental solid-state NMR...
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12-22-2011 06:50 AM
Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR.
Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR.
Consensus structure of Pf1 filamentous bacteriophage from X-ray fibre diffraction and solid-state NMR.
Eur Biophys J. 2011 Mar;40(3):221-34
Authors: Straus SK, Scott WR, Schwieters CD, Marvin DA
Filamentous bacteriophages (filamentous bacterial viruses or Inovirus) are simple and well-characterised macromolecular assemblies that are widely used in molecular biology and biophysics, both as paradigms for studying basic biological questions and as...
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[NMR paper] Assessing precision and accuracy of protein structures derived from NMR data.
Assessing precision and accuracy of protein structures derived from NMR data.
Related Articles Assessing precision and accuracy of protein structures derived from NMR data.
Proteins. 2005 Jun 1;59(4):655-61
Authors: Snyder DA, Bhattacharya A, Huang YJ, Montelione GT
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[NMR paper] Influence of internal dynamics on accuracy of protein NMR structures: derivation of r
Influence of internal dynamics on accuracy of protein NMR structures: derivation of realistic model distance data from a long molecular dynamics trajectory.
Related Articles Influence of internal dynamics on accuracy of protein NMR structures: derivation of realistic model distance data from a long molecular dynamics trajectory.
J Mol Biol. 1999 Jan 15;285(2):727-40
Authors: Schneider TR, Brünger AT, Nilges M
In order to study the effect of internal dynamics on the accuracy of NMR structures in detail, we generated NOE distance data from a...
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11-18-2010 07:05 PM
[NMR paper] An assessment of the precision and accuracy of protein structures determined by NMR.
An assessment of the precision and accuracy of protein structures determined by NMR. Dependence on distance errors.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles An assessment of the precision and accuracy of protein structures determined by NMR. Dependence on distance errors.
J Mol Biol. 1994 Jun 24;239(5):601-7
Authors: Zhao D, Jardetzky O
We tested the dependence of the accuracy and precision of calculated NMR structures on the errors of the distance constraints...
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08-22-2010 03:33 AM
[NMR paper] An assessment of the precision and accuracy of protein structures determined by NMR.
An assessment of the precision and accuracy of protein structures determined by NMR. Dependence on distance errors.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles An assessment of the precision and accuracy of protein structures determined by NMR. Dependence on distance errors.
J Mol Biol. 1994 Jun 24;239(5):601-7
Authors: Zhao D, Jardetzky O
We tested the dependence of the accuracy and precision of calculated NMR structures on the errors of the distance constraints...
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Assessing precision and accuracy of protein struct
Editor's Corner
Assessing precision and accuracy of protein structures derived from NMR data
David A. Snyder 1 2, Aneerban Bhattacharya 1 2, Yuanpeng J. Huang 1 2, Gaetano T. Montelione 1 2 *
1Center for Advanced Biotechnology and Medicine, Department of Molecular Biology and Biochemistry, and Northeast Structural Genomics Consortium, Rutgers University, Piscataway, NJ 08854
2Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Piscataway, NJ 08854
*Correspondence to Gaetano T. Montelione, CABM-Rutgers University, 679 Hoes Lane, Piscataway, NJ...
A Consensus on Protein Structure Accuracy in NMR?
Linear Mode
