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Side-chains:
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UNIO Candid
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Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
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UNIO ATNOS-Candid
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Fragment-based:
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Template-based:
GeNMR
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Refinement:
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Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
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Homology-based:
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Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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Chemical shifts re-referencing:
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Molecular dynamics:
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From structure:
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From sequence:
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Disordered proteins:
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Format conversion & validation:
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NMR sample preparation:
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Protein solubility:
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ccSOL
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camGroEL
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Isotope labeling:
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Solid-state NMR:
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Old 02-22-2016, 12:44 PM
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Default NMR assignments of mitochondrial cyclophilin Cpr3 from Saccharomyces cerevisiae.

NMR assignments of mitochondrial cyclophilin Cpr3 from Saccharomyces cerevisiae.

NMR assignments of mitochondrial cyclophilin Cpr3 from Saccharomyces cerevisiae.

Biomol NMR Assign. 2016 Feb 20;

Authors: Shukla VK, Singh JS, Trivedi D, Hosur RV, Kumar A

Abstract
Cyclophilins regulate protein folding, transport and signalling through catalysis of proline isomerization, and are ubiquitously expressed in both prokaryotes and eukaryotes. Cpr3 is the yeast mitochondrial cyclophilin and it is structurally and biophysically uncharacterized so far. Yeast cyclophilin gene cpr3 is essential for the lactate metabolism. Here, we report (1)H, (13)C, and (15)N chemical shift assignments of Cpr3 protein determined by various 2D and 3D heteronuclear NMR experiments at pH 6.5, and temperature 298*K.


PMID: 26897529 [PubMed - as supplied by publisher]



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