Developing NMR Methods to Analyse Large Proteins - Labmate Online
Developing NMR Methods to Analyse Large Proteins - Labmate Online
Developing NMR Methods to Analyse Large Proteins Labmate Online
The award will total nearly $373000 over three years to help the lab develop fast and efficient assignment methods for large proteins by NMR and make these methods accessible to the structural biology community. â??NMR spectroscopy has still a tremendous ...
TROSY NMR Spectroscopy of Large Soluble Proteins.
TROSY NMR Spectroscopy of Large Soluble Proteins.
TROSY NMR Spectroscopy of Large Soluble Proteins.
Top Curr Chem. 2011 Sep 17;
Authors: Xu Y, Matthews S
Abstract
Solution nuclear magnetic resonance spectroscopy is usually only used to study proteins with molecular weight not exceeding about 50 kDa. This size limit has been lifted significantly in recent years, thanks to the development of labelling methods and the application of transverse-relaxation optimized spectroscopy (TROSY). In particular, methyl-specific labelling and...
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09-20-2011 03:10 PM
Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins
Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins
Abstract In the last 15 years substantial advances have been made to place isotope labels in native and glycosylated proteins for NMR studies and structure determination. Key developments include segmental isotope labeling using Native Chemical Ligation, Expressed Protein Ligation and Protein Trans-Splicing. These advances are pushing the size limit of NMR spectroscopy further making larger proteins accessible for this technique. It is just emerging that segmental isotope...
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01-09-2011 12:46 PM
[NMR paper] The use of NMR chemical shifts to analyse the MD trajectories: simulation of bovine p
The use of NMR chemical shifts to analyse the MD trajectories: simulation of bovine pancreatic trypsin inhibitor dynamics in water as a test case for solvent influences.
Related Articles The use of NMR chemical shifts to analyse the MD trajectories: simulation of bovine pancreatic trypsin inhibitor dynamics in water as a test case for solvent influences.
J Pept Sci. 2003 Jul;9(7):450-60
Authors: Busetta B, Picard P, Precigoux G
In this paper the NMR secondary chemical shifts, that are estimated from a set of 3D-structures, are compared with...
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11-24-2010 09:16 PM
[NMR paper] Practical methods for solid-state NMR distance measurements on large biomolecules: co
Practical methods for solid-state NMR distance measurements on large biomolecules: constant-time rotational resonance.
Related Articles Practical methods for solid-state NMR distance measurements on large biomolecules: constant-time rotational resonance.
J Magn Reson. 1999 Aug;139(2):371-6
Authors: Balazs YS, Thompson LK
Simple modifications of the rotational resonance experiment substantially reduce the total experimental time needed to measure weak homonuclear dipolar couplings, a critical factor for achieving routine internuclear distance...
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11-18-2010 08:31 PM
[NMR paper] Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N a
Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N and 1H assignments of human carbonic anhydrase II.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N and 1H assignments of human carbonic anhydrase II.
J Mol Biol. 1996 Dec 20;264(5):1101-16
Authors: Venters RA, Farmer BT, Fierke CA, Spicer LD
Perdeuteration of all non-exchangeable proton sites can...
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08-22-2010 02:20 PM
[NMR paper] Prospects for NMR of large proteins.
Prospects for NMR of large proteins.
Related Articles Prospects for NMR of large proteins.
J Biomol NMR. 1993 Jul;3(4):375-85
Authors: Wagner G
During the last decade, solution structures of many small proteins have been solved by NMR. The size of proteins that are being analyzed by NMR seems to increase steadily. Protein structures up to 18 kD have been solved so far, and spectra of proteins up to 30 kD have been assigned. Thus, NMR emerges as an attractive technique, in particular for structural studies of proteins that cannot by...
Hadamard NMR spectroscopy for relaxation measurements of large (>35 kDa) proteins
Hadamard NMR spectroscopy for relaxation measurements of large (>35 kDa) proteins
B. Tom Burnley, Arnout P. Kalverda, Stephen J. Paisey, Alan Berry and Steve W. Homans
Journal of Biomolecular NMR; 2007; 39(3) pp 239 - 245
Abstract:
Here we present a suite of pulse sequences for the measurement of 15N T1, T1ρ and NOE data that combine traditional TROSY-based pulse sequences with band-selective Hadamard frequency encoding. The additive nature of the Hadamard matrix produces much reduced resonance overlap without the need for an increase in the dimensionality of the experiment or a...
Developing NMR Methods to Analyse Large Proteins - Labmate Online
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