[NMR paper] (1)H-detected solid-state NMR of proteins entrapped in bioinspired silica: a new tool for biomaterials characterization.
(1)H-detected solid-state NMR of proteins entrapped in bioinspired silica: a new tool for biomaterials characterization.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_npg.gif Related Articles (1)H-detected solid-state NMR of proteins entrapped in bioinspired silica: a new tool for biomaterials characterization.
Sci Rep. 2016;6:27851
Authors: Ravera E, Cerofolini L, Martelli T, Louka A, Fragai M, Luchinat C
Abstract
Proton-detection in solid-state NMR, enabled by high magnetic...
nmrlearner
Journal club
0
06-10-2016 10:49 PM
[NMR paper] CW dipolar broadening EPR spectroscopy and mechanically aligned bilayers used to measure distance and relative orientation between two TOAC spin labels on an antimicrobial peptide
CW dipolar broadening EPR spectroscopy and mechanically aligned bilayers used to measure distance and relative orientation between two TOAC spin labels on an antimicrobial peptide
Publication date: December 2014
Source:Journal of Magnetic Resonance, Volume 249</br>
Author(s): Indra D. Sahu , Eric J. Hustedt , Harishchandra Ghimire , Johnson J. Inbaraj , Robert M. McCarrick , Gary A. Lorigan</br>
An EPR membrane alignment technique was applied to measure distance and relative orientations between two spin labels on a protein oriented along the surface of the...
nmrlearner
Journal club
0
11-14-2014 08:33 AM
Engineered solubility tag for solution NMR of proteins
Engineered solubility tag for solution NMR of proteins
Abstract
The low solubility of many proteins hinders large scale expression and purification as well as biophysical measurements. Here, we devised a general strategy to solubilize a protein by conjugating it at a solvent-exposed position to a 6 kDa protein that was re-engineered to be highly soluble. We applied this method to the CARD domain of Apoptosis-associated speck-like protein containing a CARD (ASC), which represents one member of a class of proteins that are notoriously prone to aggregation. Attachment of the tag to a...
nmrlearner
Journal club
0
09-20-2013 02:39 PM
[NMR paper] Engineered solubility tag for solution NMR of proteins.
Engineered solubility tag for solution NMR of proteins.
Engineered solubility tag for solution NMR of proteins.
Protein Sci. 2013 Aug 21;
Authors: Ruschak AM, Rose JD, Coughlin MP, Religa TL
Abstract
The low solubility of many proteins hinders large scale expression and purification as well as biophysical measurements. Here, we devised a general strategy to solubilize a protein by conjugating it at a solvent exposed position to a 6 kDa protein that was re-engineered to be highly soluble. We applied this method to the CARD domain of...
nmrlearner
Journal club
0
08-23-2013 01:07 AM
Engineered solubility tag for solution NMR of proteins
Engineered solubility tag for solution NMR of proteins
Abstract
The low solubility of many proteins hinders large scale expression and purification as well as biophysical measurements. Here, we devised a general strategy to solubilize a protein by conjugating it at a solvent exposed position to a 6 kDa protein that was re-engineered to be highly soluble. We applied this method to the CARD domain of Apoptosis-associated speck-like protein containing a CARD (ASC), which represents one member of a class of proteins that are notoriously prone to aggregation. Attachment of the tag to a...
nmrlearner
Journal club
0
08-21-2013 06:36 AM
A strong 13C chemical shift signature provides the coordination mode of histidines in zinc-binding proteins
A strong 13C chemical shift signature provides the coordination mode of histidines in zinc-binding proteins
Abstract Zinc is the second most abundant metal ion incorporated in proteins, and is in many cases a crucial component of protein three-dimensional structures. Zinc ions are frequently coordinated by cysteine and histidine residues. Whereas cysteines bind to zinc via their unique Sγ atom, histidines can coordinate zinc with two different coordination modes, either Nδ1 or Nε2 is coordinating the zinc ion. The determination of this coordination mode is crucial for the accurate...
nmrlearner
Journal club
0
04-23-2012 03:31 AM
Mechanically, Magnetically, and "Rotationally Aligned" Membrane Proteins in Phospholi
Mechanically, Magnetically, and "Rotationally Aligned" Membrane Proteins in Phospholipid Bilayers Give Equivalent Angular Constraints for NMR Structure Determination.
Related Articles Mechanically, Magnetically, and "Rotationally Aligned" Membrane Proteins in Phospholipid Bilayers Give Equivalent Angular Constraints for NMR Structure Determination.
J Phys Chem B. 2010 Oct 20;
Authors: Park SH, Das BB, De Angelis AA, Scrima M, Opella SJ
The native environment for membrane proteins is the highly asymmetric phospholipid bilayer, and this has a large...
nmrlearner
Journal club
0
10-22-2010 04:33 PM
[NMR paper] Strong and weak binding of water to proteins studied by NMR triple-quantum filtered r
Strong and weak binding of water to proteins studied by NMR triple-quantum filtered relaxation spectroscopy of (17)O-water.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Strong and weak binding of water to proteins studied by NMR triple-quantum filtered relaxation spectroscopy of (17)O-water.
Biophys Chem. 1997 Sep 1;67(1-3):187-98
Authors: Torres AM, Grieve SM, Chapman BE, Kuchel PW
The triple-quantum filtered (TQF) spin-echo signal of (17)O-water, in the presence...
Bioinspired and Mechanically Strong Fibers Based on Engineered Non-Spider Chimeric Proteins
Linear Mode
