Discovery of how amyloids bind metal ions sheds light on protein function Phys.Org
â??Even though there has been a lot of high-resolution, atomic level structural work on amyloids by solid-state NMR, people have really not studied the metal-binding aspects,â?? says professor Mei Hong. Credit: Massachusetts Institute of Technology ...
Heavy metal binding domain in a cysteine-rich protein may be sea snail adaptation to metal stress - Phys.Org
Heavy metal binding domain in a cysteine-rich protein may be sea snail adaptation to metal stress - Phys.Org
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Heavy metal binding domain in a cysteine-rich protein may be sea snail adaptation to metal stress
Phys.Org
Structural Adaptation of a Protein to Increased Metal Stress: NMR Structure of a Marine Snail Metallothionein with an Additional Domain. Credit: Wiley. A special type of small sulfur-rich protein, metallothioneins, have an extraordinary capability for ...
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03-24-2017 10:00 AM
Light microscopy provides a deep look into protein structure - Phys.org - Phys.Org
Light microscopy provides a deep look into protein structure - Phys.org - Phys.Org
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Phys.Org
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Light microscopy provides a deep look into protein structure - Phys.org
Phys.Org
Light microscopy continues to reveal the microscopic world at an ever increasing resolution. Using a new method coined COLD, scientists at the Max Planck ...
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01-25-2017 11:13 PM
Study Sheds Light On Structure of Alzheimer Fibrils - Scicasts (press release) (blog)
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Study Sheds Light On Structure of Alzheimer Fibrils
Scicasts (press release) (blog)
Only solid-state nuclear magnetic resonance spectroscopy (solid-state NMR) is capable of offering a view at the atomic level in this case. New developments in methods made it possible to measure a network of distances between the atoms in the protein ...
Study Sheds Light On Structure of Alzheimer Fibrils - Scicasts (press release) (blog)
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Research discovery: Near-complete set of templates for protein complexes ... - Phys.Org
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Research discovery: Near-complete set of templates for protein complexes ...
Phys.Org
Such accurate computer modeling is based on â??templateâ?? structures of proteins determined by X-ray crystallography and nuclear magnetic resonance. Until now, it was believed that many years of work were required before a practically useful set of ...
Research discovery: Near-complete set of templates for protein complexes ... - Phys.Org
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06-08-2012 08:47 PM
Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins
Maximum occurrence analysis of protein conformations for different distributions of paramagnetic metal ions within flexible two-domain proteins
Publication year: 2011
Source: Journal of Magnetic Resonance, Available online 30 December 2011</br>
Claudio*Luchinat, Malini*Nagulapalli, Giacomo*Parigi, Luca*Sgheri</br>
Multidomain proteins are composed of rigid domains connected by (flexible) linkers. Therefore, the domains may experience a large degree of reciprocal reorientation. Pseudocontact shifts and residual dipolar couplings arising from one or more paramagnetic metals successively...
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12-31-2011 10:40 AM
[NMR paper] Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge
Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate.
Related Articles Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate.
J Biol Chem. 2002 Apr 5;277(14):12375-81
Authors: Odaert B, Landrieu I, Dijkstra K, Schuurman-Wolters G, Casteels P, Wieruszeski JM, Inze D, Scheek R, Lippens G
Cyclin-dependent kinase subunit (CKS) proteins bind to cyclin-dependent...
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11-24-2010 08:49 PM
[NMR paper] Lanthanide ions bind specifically to an added "EF-hand" and orient a membrane protein
Lanthanide ions bind specifically to an added "EF-hand" and orient a membrane protein in micelles for solution NMR spectroscopy.
Related Articles Lanthanide ions bind specifically to an added "EF-hand" and orient a membrane protein in micelles for solution NMR spectroscopy.
J Magn Reson. 2000 Oct;146(2):381-4
Authors: Ma C, Opella SJ
Twelve amino acid residues corresponding to an "EF-hand" calcium-binding site were added to the N-terminus of a protein, providing a specific lanthanide ion binding that weakly orients the protein in solution. A...