[NMR paper] NMR of intrinsically disordered proteins: A note on the application of (15)N-(13)C(alpha) het-TOCSY mixing for (13)C(alpha) magnetisation transfers
Intrinsically disordered proteins (IDPs) or protein regions represent functionally important biomolecules without unique structure. Their inherent flexibility prevents high-resolution structure determination by X-ray or cryo-EM methods. In contrast, NMR spectroscopy provides an extensive and still growing set of experimental approaches to obtain detailed information on structure and dynamics of IDPs. Here, it is experimentally demonstrated that ^(15)N-^(13)C^(?) band-selective heteronuclear...
[NMR paper] Application of NMR to studies of intrinsically disordered proteins.
Application of NMR to studies of intrinsically disordered proteins.
Related Articles Application of NMR to studies of intrinsically disordered proteins.
Arch Biochem Biophys. 2017 May 11;:
Authors: Gibbs EB, Cook EC, Showalter SA
Abstract
The prevalence of intrinsically disordered protein regions, particularly in eukaryotic proteins, and their clear functional advantages for signaling and gene regulation have created an imperative for high-resolution structural and mechanistic studies. NMR spectroscopy has played a central role...
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Application of NMR to studies of intrinsically disordered proteins
Application of NMR to studies of intrinsically disordered proteins
Publication date: Available online 11 May 2017
Source:Archives of Biochemistry and Biophysics</br>
Author(s): Eric B. Gibbs, Erik C. Cook, Scott A. Showalter</br>
The prevalence of intrinsically disordered protein regions, particularly in eukaryotic proteins, and their clear functional advantages for signaling and gene regulation have created an imperative for high-resolution structural and mechanistic studies. NMR spectroscopy has played a central role in enhancing not only our understanding of...
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05-12-2017 05:13 PM
HN-NCA heteronuclear TOCSY-NH experiment for 1 H N and 15 N sequential correlations in ( 13 C, 15 N) labelled intrinsically disordered proteins
HN-NCA heteronuclear TOCSY-NH experiment for 1 H N and 15 N sequential correlations in ( 13 C, 15 N) labelled intrinsically disordered proteins
Abstract
A simple triple resonance NMR experiment that leads to the correlation of the backbone amide resonances of each amino acid residue â??iâ?? with that of residues â??iâ??1â?? and â??i+1â?? in (13C, 15N) labelled intrinsically disordered proteins (IDPs) is presented. The experimental scheme, {HN-NCA heteronuclear TOCSY-NH}, exploits the favourable relaxation properties of IDPs and the presence of 1 ...
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08-18-2015 10:07 AM
[NMR paper] Comparison of residual alpha- and beta-structures between two intrinsically disordered proteins by using NMR.
Comparison of residual alpha- and beta-structures between two intrinsically disordered proteins by using NMR.
Comparison of residual alpha- and beta-structures between two intrinsically disordered proteins by using NMR.
Biochim Biophys Acta. 2014 Dec 15;
Authors: Ono Y, Miyashita M, Ono Y, Okazaki H, Watanabe S, Tochio N, Kigawa T, Nishimura C
Abstract
Intrinsically disordered proteins contain some residual structures, which may fold further upon binding to the partner protein for function. The residual structures observed in...
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12-20-2014 06:30 PM
Comparison of residual alpha- and beta-structures between two intrinsically disordered proteins by using NMR
Comparison of residual alpha- and beta-structures between two intrinsically disordered proteins by using NMR
Publication date: Available online 15 December 2014
Source:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics</br>
Author(s): Yu-ichi Ono , Manami Miyashita , Yumi Ono , Honoka Okazaki , Satoru Watanabe , Naoya Tochio , Takanori Kigawa , Chiaki Nishimura</br>
Intrinsically disordered proteins contain some residual structures, which may fold further upon binding to the partner protein for function. The residual structures observed in two...
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12-16-2014 03:47 AM
A six-dimensional alpha proton detection-based APSY experiment for backbone assignment of intrinsically disordered proteins
A six-dimensional alpha proton detection-based APSY experiment for backbone assignment of intrinsically disordered proteins
Abstract
Sequence specific resonance assignment is the prerequisite for the NMR-based analysis of the conformational ensembles and their underlying dynamics of intrinsically disordered proteins. However, rapid solvent exchange in intrinsically disordered proteins often complicates assignment strategies based on HN-detection. Here we present a six-dimensional alpha proton detection-based automated projection spectroscopy (APSY)...
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11-04-2014 01:02 AM
[NMR paper] Structure-based minimization of transforming growth factor-alpha (TGF-alpha) through
Structure-based minimization of transforming growth factor-alpha (TGF-alpha) through NMR analysis of the receptor-bound ligand. Design, solution structure, and activity of TGF-alpha 8-50.
Related Articles Structure-based minimization of transforming growth factor-alpha (TGF-alpha) through NMR analysis of the receptor-bound ligand. Design, solution structure, and activity of TGF-alpha 8-50.
J Biol Chem. 1998 Oct 16;273(42):27357-63
Authors: McInnes C, Wang J, Al Moustafa AE, Yansouni C, O'Connor-McCourt M, Sykes BD
The investigation of a...
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11-17-2010 11:15 PM
[NMR paper] Combined use of 13C chemical shift and 1H alpha-13C alpha heteronuclear NOE data in m
Combined use of 13C chemical shift and 1H alpha-13C alpha heteronuclear NOE data in monitoring a protein NMR structure refinement.
Related Articles Combined use of 13C chemical shift and 1H alpha-13C alpha heteronuclear NOE data in monitoring a protein NMR structure refinement.
J Biomol NMR. 1995 Feb;5(2):161-72
Authors: Celda B, Biamonti C, Arnau MJ, Tejero R, Montelione GT
A large portion of the 13C resonance assignments for murine epidermal growth factor (mEGF) at pH 3.1 and 28 degrees C has been determined at natural isotope abundance....
NMR of intrinsically disordered proteins: A note on the application of (15)N-(13)C(alpha) het-TOCSY mixing for (13)C(alpha) magnetisation transfers
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