Backbone (1)H, (15)N, (13)C and side chain (13)C? NMR chemical shift assignment of murine interleukin-10.
Biomol NMR Assign. 2013 Aug 25;
Authors: Künze G, Theisgen S, Huster D
Abstract
Almost complete assignment of backbone (1)H, (13)C, (15)N and side chain (13)C? resonances for the immune-regulatory cytokine IL-10 is reported. The protein was overexpressed in Escherichia coli and was refolded from inclusion bodies. The point mutation C149Y was introduced to suppress incorrect disulfide bond formation and to improve protein refolding.
PMID: 23982919 [PubMed - as supplied by publisher]
[NMR paper] Practical use of chemical shift databases for protein solid-state NMR: 2D chemical shift maps and amino-acid assignment with secondary-structure information.
Practical use of chemical shift databases for protein solid-state NMR: 2D chemical shift maps and amino-acid assignment with secondary-structure information.
Practical use of chemical shift databases for protein solid-state NMR: 2D chemical shift maps and amino-acid assignment with secondary-structure information.
J Biomol NMR. 2013 Apr 28;
Authors: Fritzsching KJ, Yang Y, Schmidt-Rohr K, Hong M
Abstract
We introduce a Python-based program that utilizes the large database of (13)C and (15)N chemical shifts in the Biological Magnetic...
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04-30-2013 10:21 PM
[NMR paper] Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain.
Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain.
Biomol NMR Assign. 2013 Jan 22;
Authors: Orbán-Németh Z, Henen MA, Geist L, Zerko S, Saxena S, Stanek J, Ko?mi?ski W, Propst F, Konrat R
Abstract
Microtubule-associated protein 1B (MAP1B) is a classical...
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02-03-2013 10:19 AM
PPM: a side-chain and backbone chemical shift predictor for the assessment of protein conformational ensembles
PPM: a side-chain and backbone chemical shift predictor for the assessment of protein conformational ensembles
Abstract The combination of the wide availability of protein backbone and side-chain NMR chemical shifts with advances in understanding of their relationship to protein structure makes these parameters useful for the assessment of structural-dynamic protein models. A new chemical shift predictor (PPM) is introduced, which is solely based on physicalâ??chemical contributions to the chemical shifts for both the protein backbone and methyl-bearing amino-acid side chains. To...
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09-15-2012 09:04 AM
Protein side-chain resonance assignment and NOE assignment using RDC-defined backbones without TOCSY data
Protein side-chain resonance assignment and NOE assignment using RDC-defined backbones without TOCSY data
Abstract One bottleneck in NMR structure determination lies in the laborious and time-consuming process of side-chain resonance and NOE assignments. Compared to the well-studied backbone resonance assignment problem, automated side-chain resonance and NOE assignments are relatively less explored. Most NOE assignment algorithms require nearly complete side-chain resonance assignments from a series of through-bond experiments such as HCCH-TOCSY or HCCCONH. Unfortunately, these TOCSY...
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06-27-2011 04:30 AM
Site-specific (19)F NMR chemical shift and side chain relaxation analysis of a membra
Site-specific (19)F NMR chemical shift and side chain relaxation analysis of a membrane protein labeled with an unnatural amino acid.
Related Articles Site-specific (19)F NMR chemical shift and side chain relaxation analysis of a membrane protein labeled with an unnatural amino acid.
Protein Sci. 2010 Nov 15;
Authors: Shi P, Wang H, Xi Z, Shi C, Xiong Y, Tian C
Site-specific (19)F chemical shift and side chain relaxation analysis can be applied on large size proteins. Here, one dimensional (19)F spectra and T(1), T(2) relaxation data were acquired...
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11-17-2010 05:49 PM
Site-Specific Protein Backbone and Side-Chain NMR Chemical Shift and Relaxation Analy
Site-Specific Protein Backbone and Side-Chain NMR Chemical Shift and Relaxation Analysis of Human Vinexin SH3 Domain using a Genetically Encoded (15)N/(19)F-Labeled Unnatural Amino Acid.
Related Articles Site-Specific Protein Backbone and Side-Chain NMR Chemical Shift and Relaxation Analysis of Human Vinexin SH3 Domain using a Genetically Encoded (15)N/(19)F-Labeled Unnatural Amino Acid.
Biochem Biophys Res Commun. 2010 Oct 11;
Authors: Shi P, Xi Z, Wang H, Shi C, Xiong Y, Tian C
SH3 is a ubiquitous domain mediating protein-protein interactions....
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10-16-2010 03:56 PM
[NMR paper] Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double
Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy.
Related Articles Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy.
Biochemistry. 1990 Sep 4;29(35):8172-84
Authors: Clore GM, Bax A, Driscoll PC, Wingfield PT, Gronenborn AM
The assignment of the aliphatic 1H and 13C resonances of IL-1 beta, a protein of 153 residues and molecular...
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08-21-2010 11:04 PM
[NMR paper] Complete resonance assignment for the polypeptide backbone of interleukin 1 beta usin
Complete resonance assignment for the polypeptide backbone of interleukin 1 beta using three-dimensional heteronuclear NMR spectroscopy.
Related Articles Complete resonance assignment for the polypeptide backbone of interleukin 1 beta using three-dimensional heteronuclear NMR spectroscopy.
Biochemistry. 1990 Apr 10;29(14):3542-56
Authors: Driscoll PC, Clore GM, Marion D, Wingfield PT, Gronenborn AM
The complete sequence-specific assignment of the 15N and 1H backbone resonances of the NMR spectrum of recombinant human interleukin 1 beta (153...
Backbone (1)H, (15)N, (13)C and side chain (13)C? NMR chemical shift assignment of murine interleukin-10.
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