[NMR paper] Rapid Identification of Amino Acid types in Proteins using phase modulated 2D HN(CACB) and 2D HN(COCACB)
Rapid Identification of Amino Acid types in Proteins using phase modulated 2D HN(CACB) and 2D HN(COCACB)
Publication date: Available online 7 April 2016
Source:Journal of Magnetic Resonance</br>
Author(s): Abhinav Dubey, Somnath Mondal, Kousik Chandra, Hanudatta S. Atreya</br>
We present a simple approach to rapidly identify amino acid types in proteins from a 2D spectrum. The method is based on the fact that 13C? chemical shifts of different amino acid types fall in distinct spectral regions. By evolving the 13C chemical shifts in the conventional HNCACB or...
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04-08-2016 01:05 PM
Amino acid recognition for automatic resonance assignment of intrinsically disordered proteins
Amino acid recognition for automatic resonance assignment of intrinsically disordered proteins
Abstract
Resonance assignment is a prerequisite for almost any NMR-based study of proteins. It can be very challenging in some cases, however, due to the nature of the protein under investigation. This is the case with intrinsically disordered proteins, for example, whose NMR spectra suffer from low chemical shifts dispersion and generally low resolution. For these systems, sequence specific assignment is highly time-consuming, so the prospect of using...
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02-19-2016 08:39 AM
Paramagnetic relaxation enhancement of membrane proteins by incorporation of the metal-chelating unnatural amino acid 2-amino-3-(8-hydroxyquinolin-3-yl)propanoic acid (HQA)
Paramagnetic relaxation enhancement of membrane proteins by incorporation of the metal-chelating unnatural amino acid 2-amino-3-(8-hydroxyquinolin-3-yl)propanoic acid (HQA)
Abstract
The use of paramagnetic constraints in protein NMR is an active area of research because of the benefits of long-range distance measurements (>10Â*Ã?). One of the main issues in successful execution is the incorporation of a paramagnetic metal ion into diamagnetic proteins. The most common metal ion tags are relatively long aliphatic chains attached to the side chain of a...
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11-28-2014 11:37 AM
Movements of proteins can be predicted from their amino acid sequence - HealthCanal.com
Movements of proteins can be predicted from their amino acid sequence - HealthCanal.com
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Movements of proteins can be predicted from their amino acid sequence
HealthCanal.com
Researchers of the VIB department of Structural Biology, in a collaboration within the 'Interuniversity Institute of Bioinformatics in Brussels (IB2)', have developed a method to predict how much the backbone chain of a protein moves based on only its ...
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11-26-2013 01:19 AM
[NMR paper] A suite of amino acid residue type classification pulse sequences for 13C-detected NMR of proteins
A suite of amino acid residue type classification pulse sequences for 13C-detected NMR of proteins
Publication date: Available online 10 July 2013
Source:Journal of Magnetic Resonance</br>
Author(s): David Pantoja-Uceda , Jorge Santoro</br>
A suite of 13C-detected NMR pulse sequences to edit the correlation peaks of the CACO and CON spectra according to the amino acid residue type is presented. The pulse sequences exploit the topology of the C? carbon and led to the sorting of the CACO or CON signals into several classes depending on the nature of the generating...
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07-11-2013 12:07 PM
[NMR paper] Amino Acid-Selective Segmental Isotope Labeling of Multidomain Proteins for Structural Biology.
Amino Acid-Selective Segmental Isotope Labeling of Multidomain Proteins for Structural Biology.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Amino Acid-Selective Segmental Isotope Labeling of Multidomain Proteins for Structural Biology.
Chembiochem. 2013 Jan 30;
Authors: Michel E, Skrisovska L, Wüthrich K, Allain FH
Abstract
Current solution NMR techniques enable structural investigations of proteins in molecular particles with sizes...
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02-03-2013 10:19 AM
Amino acid selective unlabeling for sequence specific resonance assignments in proteins
Amino acid selective unlabeling for sequence specific resonance assignments in proteins
Abstract Sequence specific resonance assignment constitutes an important step towards high-resolution structure determination of proteins by NMR and is aided by selective identification and assignment of amino acid types. The traditional approach to selective labeling yields only the chemical shifts of the particular amino acid being selected and does not help in establishing a link between adjacent residues along the polypeptide chain, which is important for sequential assignments. An alternative...
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03-20-2012 12:42 AM
Automated amino acid side-chain NMR assignment of proteins using 13C- and 15N-resolved 3D [1H,1H]-NOESY
Automated amino acid side-chain NMR assignment of proteins using 13C- and 15N-resolved 3D -NOESY
Francesco Fiorito, Torsten Herrmann, Fred F. Damberger and Kurt Wüthrich
Journal of Biomolecular NMR; 2008; 42(1); pp 23-33
Abstract
ASCAN is a new algorithm for automatic sequence-specific NMR assignment of amino acid side-chains in proteins, which uses as input the primary structure of the protein, chemical shift lists of 1HN, 15N, 13Cα, 13Cβ and possibly 1Hα from the previous polypeptide backbone assignment, and one or several 3D 13C- or 15N-resolved -NOESY spectra. ASCAN has also been...
In-vivo production of diverse ?-amino acid-containing proteins
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