Arachnid Rapunzel: Researchers spin spider silk proteins into artificial silk - (e) Science News
Arachnid Rapunzel: Researchers spin spider silk proteins into artificial silk - (e) Science News
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Arachnid Rapunzel: Researchers spin spider silk proteins into artificial silk
(e) Science News
Jan Rainey's group at Dalhousie University used nuclear magnetic resonance (NMR) spectroscopy to analyze the structure of AcSp1's repeat sequence at very high resolution, producing one of the first spider silk repeat...
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02-12-2015 06:10 AM
[NMR paper] Observation of scalar nuclear spin-spin coupling in van der Waals complexes.
From Mendeley Biomolecular NMR group:
Observation of scalar nuclear spin-spin coupling in van der Waals complexes.
Proceedings of the National Academy of Sciences of the United States of America (2012). Volume: 109, Issue: 31. Pages: 12393-7. Micah P Ledbetter, Giacomo Saielli, Alessandro Bagno, Nhan Tran, Michael V Romalis et al.
Scalar couplings between covalently bound nuclear spins are a ubiquitous feature in nuclear magnetic resonance (NMR) experiments, imparting valuable information to NMR spectra regarding molecular structure and conformation. Such couplings arise due to a...
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09-09-2014 03:44 PM
[NMR paper] Electron Spin Density on the Axial His Ligand of High-Spin and Low-Spin Nitrophorin 2 Probed by Heteronuclear NMR Spectroscopy.
Electron Spin Density on the Axial His Ligand of High-Spin and Low-Spin Nitrophorin 2 Probed by Heteronuclear NMR Spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Electron Spin Density on the Axial His Ligand of High-Spin and Low-Spin Nitrophorin 2 Probed by Heteronuclear NMR Spectroscopy.
Inorg Chem. 2013 Jan 17;
Authors: Abriata LA, Zaballa ME, Berry RE, Yang F, Zhang H, Walker FA, Vila AJ
Abstract
The electronic structure of heme proteins is exquisitely tuned...
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02-03-2013 10:19 AM
[NMR paper] Observation of scalar nuclear spin-spin coupling in van der Waals complexes.
From Mendeley Biomolecular NMR group:
Observation of scalar nuclear spin-spin coupling in van der Waals complexes.
Proceedings of the National Academy of Sciences of the United States of America (2012). Volume: 109, Issue: 31. Pages: 12393-7. Micah P Ledbetter, Giacomo Saielli, Alessandro Bagno, Nhan Tran, Michael V Romalis et al.
Scalar couplings between covalently bound nuclear spins are a ubiquitous feature in nuclear magnetic resonance (NMR) experiments, imparting valuable information to NMR spectra regarding molecular structure and conformation. Such couplings arise due to a...
nmrlearner
Journal club
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11-22-2012 11:49 AM
Uncovering symmetry-breaking vector and reliability order for assigning secondary structures of proteins from atomic NMR chemical shifts in amino acids
Uncovering symmetry-breaking vector and reliability order for assigning secondary structures of proteins from atomic NMR chemical shifts in amino acids
Abstract Unravelling the complex correlation between chemical shifts of 13 C α, 13 C β, 13 C�, 1 H α, 15 N, 1 H N atoms in amino acids of proteins from NMR experiment and local structural environments of amino acids facilitates the assignment of secondary structures of proteins. This is an important impetus for both determining the three-dimensional structure and understanding the biological function of proteins. The previous...
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11-14-2011 08:45 AM
Structural biology: Breaking the protein rules - Nature.com (subscription)
Structural biology: Breaking the protein rules - Nature.com (subscription)
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Nature.com (subscription)
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Structural biology: Breaking the protein rules
Nature.com (subscription)
As is Martin Blackledge, an NMR spectroscopist at the Institute of Structural Biology in Grenoble, France, who compares the excitement now to that surrounding the first crystal protein structures in the 1950s. "Every new case is fascinating at the ...
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03-10-2011 04:29 AM
[NMR900 blog] Nature News: Breaking the protein rules
Nature News: Breaking the protein rules
One of the textbook concepts in molecular biology is that proteins fold up spontaneously to form the most energetically stable three-dimensional structures. These folded proteins are presumed structurally rigid, which is important for their unique functionality, e.g. as enzymes. There are indications, however, mostly coming from NMR studies, that many important proteins exist in disordered form. A news feature in the latest issue of Nature discusses implications of this potentially far-reaching finding. Among cited examples of intrinsically...
Breaking News: The End of Spin ... and of The Universe
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