[NMR paper] Short two-armed lanthanide-binding tags for paramagnetic NMR spectroscopy based on chiral 1,4,7,10-tetrakis(2-hydroxypropyl)-1,4,7,10-tetraazacyclododecane scaffolds.
Short two-armed lanthanide-binding tags for paramagnetic NMR spectroscopy based on chiral 1,4,7,10-tetrakis(2-hydroxypropyl)-1,4,7,10-tetraazacyclododecane scaffolds.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Short two-armed lanthanide-binding tags for paramagnetic NMR spectroscopy based on chiral 1,4,7,10-tetrakis(2-hydroxypropyl)-1,4,7,10-tetraazacyclododecane scaffolds.
Chem Commun (Camb). 2017 Nov 22;:
Authors: Lee MD, Dennis ML, Graham B, Swarbrick JD
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[NMR paper] Structure-based design of scaffolds targeting PDE10A by INPHARMA-NMR.
Structure-based design of scaffolds targeting PDE10A by INPHARMA-NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Structure-based design of scaffolds targeting PDE10A by INPHARMA-NMR.
J Chem Inf Model. 2017 May 31;:
Authors: Codutti L, Grimaldi M, Carlomagno T
Abstract
Phosphodiesterases (PDE) hydrolyze both cyclic AMP and GMP (cAMP/cGMP) and are responsible for the regulation of their levels in a multitude of cellular functions. PDE10A is...
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De novo protein structure determination from near-atomic-resolution cryo-EM maps - Nature.com
De novo protein structure determination from near-atomic-resolution cryo-EM maps - Nature.com
<img alt="" height="1" width="1">
De novo protein structure determination from near-atomic-resolution cryo-EM maps
Nature.com
Despite these developments, little progress has been made in de novo model building into near-atomic-resolution cryo-EM density maps. Structural interpretation of cryo-EM maps typically starts with fitting an atomic X-ray or NMR structure into the map5.
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[NMR paper] Optimization of the methods for small peptide solution structure determination by NMR spectroscopy
From Mendeley Biomolecular NMR group:
Optimization of the methods for small peptide solution structure determination by NMR spectroscopy
Mol Biol (Mosk) (2010). Volume: 44, Issue: 6. Pages: 1075-1085. A N Istrate, A B Mantsyzov, S A Kozin, V I Pol'shakov et al.
NMR spectroscopy was recognized as a method of protein structure determination in solution. However, determination of the conformation of small peptides, which undergo fast molecular motions, remains a challenge. This is mainly caused by impossibility to collect required quantity of the distance and dihedral angle restraints...
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[NMR paper] Optimization of the methods for small peptide solution structure determination by NMR spectroscopy
From Mendeley Biomolecular NMR group:
Optimization of the methods for small peptide solution structure determination by NMR spectroscopy
Mol Biol (Mosk) (2010). Volume: 44, Issue: 6. Pages: 1075-1085. A N Istrate, A B Mantsyzov, S A Kozin, V I Pol'shakov et al.
NMR spectroscopy was recognized as a method of protein structure determination in solution. However, determination of the conformation of small peptides, which undergo fast molecular motions, remains a challenge. This is mainly caused by impossibility to collect required quantity of the distance and dihedral angle restraints...
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10-12-2012 09:58 AM
[NMR paper] Optimization of the methods for small peptide solution structure determination by NMR spectroscopy
From Mendeley Biomolecular NMR group:
Optimization of the methods for small peptide solution structure determination by NMR spectroscopy
Mol Biol (Mosk) (2010). Volume: 44, Issue: 6. Pages: 1075-1085. A N Istrate, A B Mantsyzov, S A Kozin, V I Pol'shakov et al.
NMR spectroscopy was recognized as a method of protein structure determination in solution. However, determination of the conformation of small peptides, which undergo fast molecular motions, remains a challenge. This is mainly caused by impossibility to collect required quantity of the distance and dihedral angle restraints...
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[Optimization of the methods for small peptide solution structure determination by NMR spectroscopy].
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Mol Biol (Mosk). 2010 Nov-Dec;44(6):1075-85
Authors:
NMR spectroscopy was recognized as a method of protein structure determination in solution. However, determination of the conformation of small peptides, which undergo fast molecular motions, remains a challenge. This is mainly caused by impossibility to collect required quantity of the distance and dihedral angle restraints from NMR spectra. At the same time, short charged peptides play an important role in a number of biological processes, in particular in pathogenesis of neurodegenerative...