Tool narrows search for elusive protein structures Spectrum
Techniques such as X-ray crystallography and nuclear magnetic resonance spectroscopy have revealed the structures of proteins in about a third of these families. Computer models have determined the shapes in nearly an additional third based on their ...
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http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja504577t/aop/images/medium/ja-2014-04577t_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja504577t
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/V2rZJxvuMXQ
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08-02-2014 12:38 PM
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Protein NMR Structures Refined with Rosetta Have Higher Accuracy Relative to Corresponding X-ray Crystal Structures.
J Am Chem Soc. 2014 Jan 6;
Authors: Mao B, Tejero R, Baker D, Montelione GT
Abstract
We have found that refinement of protein NMR structures using Rosetta with experimental NMR restraints yields more accurate protein NMR structures than those that have been deposited in the PDB using standard refinement...
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01-08-2014 11:23 AM
The Elusive Structure of Pd2(dba)3. Examination by Isotopic Labeling, NMR Spectroscopy, and X-rayDiffraction Analysis: Synthesis and Characterization of Pd2(dba-Z)3 Complexes
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http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja403259c/aop/images/medium/ja-2013-03259c_0018.gif
Journal of the American Chemical Society
DOI: 10.1021/ja403259c...
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05-24-2013 08:54 AM
NMR as a tool to identify and characterize protein folding intermediates
NMR as a tool to identify and characterize protein folding intermediates
Available online 12 September 2012
Publication year: 2012
Source:Archives of Biochemistry and Biophysics</br>
</br>
NMR spectroscopy is one of the few biophysical methods that can provide atomic-level insight into the conformation of partially folded states and/or intermediates present along the protein folding pathway. Such studies are important not only within the context of the protein folding problem, but also to push forward the technique, due to the challenging nature of the systems studied....
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NMR as a Unique Tool in Assessment and Complex Determination of Weak Protein-Protein Interactions.
NMR as a Unique Tool in Assessment and Complex Determination of Weak Protein-Protein Interactions.
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Top Curr Chem. 2011 Aug 2;
Authors: Vinogradova O, Qin J
Protein-protein interactions are crucial for a wide variety of biological processes. These interactions range from high affinity (K (d) < nM) to very low affinity (K (d) > mM). While much is known about the nature of high affinity protein complexes, our knowledge about structural characteristics...
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08-03-2011 12:00 PM
[NMR paper] Reconsidering complete search algorithms for protein backbone NMR assignment.
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Bioinformatics. 2005 Sep 1;21 Suppl 2:ii230-6
Authors: Vitek O, Bailey-Kellogg C, Craig B, Kuliniewicz P, Vitek J
MOTIVATION: Nuclear magnetic resonance (NMR) spectroscopy is widely used to determine and analyze protein structures. An essential step in NMR studies is determining the backbone resonance assignment, which maps individual atoms to experimentally measured...
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12-01-2010 06:56 PM
[NMR paper] Comparison of X-ray and NMR structures: is there a systematic difference in residue contacts between X-ray- and NMR-resolved protein structures?
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Proteins. 2005 Jul 1;60(1):139-47
Authors: Garbuzynskiy SO, Melnik BS, Lobanov MY, Finkelstein AV, Galzitskaya OV
We have compared structures of 78 proteins determined by both NMR and X-ray methods. It is shown that X-ray and NMR structures...