Introduction Sensitive methods are necessary to identify the residual structure in an unfolded protein, which may be similar to the functionally native structure. Signal intensity in NMR experiments is useful for analyzing the line width for a dynamic structure; however, another contribution is contained. Methods Here, the signal-intensity difference along the sequence was used for probability to calculate the standard deviation. Results The relative values of the standard deviations were 0.57,...
[NMR paper] Residual Structure of Unfolded Ubiquitin as Revealed by Hydrogen/Deuterium-Exchange 2D NMR.
Residual Structure of Unfolded Ubiquitin as Revealed by Hydrogen/Deuterium-Exchange 2D NMR.
Related Articles Residual Structure of Unfolded Ubiquitin as Revealed by Hydrogen/Deuterium-Exchange 2D NMR.
Biophys J. 2020 Oct 14;:
Authors: Yagi-Utsumi M, Chandak MS, Yanaka S, Hiranyakorn M, Nakamura T, Kato K, Kuwajima K
Abstract
The characterization of residual structures persistent in unfolded proteins in concentrated denaturant solution is currently an important issue in studies of protein folding because the residual structure...
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[NMR paper] Distinct residual and disordered structures of alpha-synuclein analyzed by amide-proton exchange and NMR signal intensity.
Distinct residual and disordered structures of alpha-synuclein analyzed by amide-proton exchange and NMR signal intensity.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/https:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Distinct residual and disordered structures of alpha-synuclein analyzed by amide-proton exchange and NMR signal intensity.
Biochim Biophys Acta Proteins Proteom. 2020 Jun 01;:140464
Authors: Okuwaki R, Shinmura I, Morita S, Matsugami A, Hayashi F, Goto Y, Nishimura C
Abstract
...
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[NMR paper] NMR Characterization of the Near Native and Unfolded States of the PTB Domain of Dok1: Alternate Conformations and Residual Clusters.
NMR Characterization of the Near Native and Unfolded States of the PTB Domain of Dok1: Alternate Conformations and Residual Clusters.
Related Articles NMR Characterization of the Near Native and Unfolded States of the PTB Domain of Dok1: Alternate Conformations and Residual Clusters.
PLoS One. 2014;9(2):e90557
Authors: Gupta S, Bhattacharjya S
Abstract
BACKGROUND: Phosphotyrosine binding (PTB) domains are critically involved in cellular signaling and diseases. PTB domains are categorized into three distinct structural classes namely...
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[Question from NMRWiki Q&A forum] Macro available that can determine the standard deviation of the spectral noise for a many similar 2D spectra
Macro available that can determine the standard deviation of the spectral noise for a many similar 2D spectra
Hi !
I need a macro that can determine the standard deviation of the spectral noise for a manysimilar 2D spectra.
I have 75 spectra obtained for an R1-rho experiment.Each spectra has an alteration for either of the varian parameter:deltadof2, dpwr2slock or ncyc.
I use NMRPipe seriesTab to acquire the peak height for each spectrum.I use relax (http://nmr-relax.com) to perform the analysis.
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09-16-2013 05:07 PM
Residual interactions in unfolded bile acid-binding protein by (19) F NMR.
Residual interactions in unfolded bile acid-binding protein by (19) F NMR.
Residual interactions in unfolded bile acid-binding protein by (19) F NMR.
Protein Sci. 2011 Feb;20(2):327-35
Authors: Basehore HK, Ropson IJ
The folding initiation mechanism of human bile acid-binding protein (BABP) has been examined by (19) F NMR. Equilibrium unfolding studies of BABP labeled with fluorine at all eight of its phenylalanine residues showed that at least two sites experience changes in solvent exposure at high denaturant concentrations. Peak...
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Residual interactions in unfolded bile acid-binding protein by (19)F-NMR.
Residual interactions in unfolded bile acid-binding protein by (19)F-NMR.
Related Articles Residual interactions in unfolded bile acid-binding protein by (19)F-NMR.
Protein Sci. 2010 Nov 29;
Authors: Basehore HK, Ropson IJ
The folding initiation mechanism of human bile acid-binding protein (BABP) has been examined by (19)F-NMR. Equilibrium unfolding studies of BABP labeled with fluorine at all eight of its phenylalanine residues showed that at least two sites experience changes in solvent exposure at high denaturant concentrations. Peak assignments...
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12-01-2010 04:41 PM
[NMR paper] Probing residual interactions in unfolded protein states using NMR spin relaxation te
Probing residual interactions in unfolded protein states using NMR spin relaxation techniques: an application to delta131delta.
Related Articles Probing residual interactions in unfolded protein states using NMR spin relaxation techniques: an application to delta131delta.
J Am Chem Soc. 2003 Oct 1;125(39):11988-92
Authors: Choy WY, Kay LE
Residual interactions in delta131delta, a large disordered fragment of staphylococcal nuclease, have been probed at two different pHs using backbone (15)N and side-chain methyl (2)H NMR spin relaxation...
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Theoretical framework for NMR residual dipolar couplings in unfolded proteins
Theoretical framework for NMR residual dipolar couplings in unfolded proteins
O. I. Obolensky, Kai Schlepckow, Harald Schwalbe and A. V. Solov’yov
Journal of Biomolecular NMR; 2007; 39(1) pp 1-16
Abstract:
A theoretical framework for the prediction of nuclear magnetic resonance (NMR) residual dipolar couplings (RDCs) in unfolded proteins under weakly aligning conditions is presented. The unfolded polypeptide chain is modeled as a random flight chain while the alignment medium is represented by a set of regularly arranged obstacles. For the case of bicelles oriented perpendicular to...