Most techniques allow detection of protein unfolding either by following the behaviour of single reporters or as an averaged all-or-none process. We recently added 2D NMR spectroscopy to the well-established techniques able to obtain information on the process of unfolding using resonances of residues in the hydrophobic core of a protein. Here, we questioned whether an analysis of the individual stability curves from each resonance could provide additional site-specific information. We used the...
Site-Specific Protein Internal Motions Revealed by 2H Solid-State NMR Spectroscopy
Site-Specific Protein Internal Motions Revealed by 2H Solid-State NMR Spectroscopy
Publication date: 16 February 2016
Source:Biophysical Journal, Volume 110, Issue 3, Supplement 1</br>
Author(s): Xiangyan Shi, Deborah A. Berthold, Chad M. Rienstra</br>
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02-17-2016 07:50 PM
[NMR paper] Site-Specific Internal Motions in GB1 Protein Microcrystals Revealed by 3D (2)H-(13)C-(13)C Solid-State NMR Spectroscopy.
Site-Specific Internal Motions in GB1 Protein Microcrystals Revealed by 3D (2)H-(13)C-(13)C Solid-State NMR Spectroscopy.
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J Am Chem Soc. 2016 Feb 5;
Authors: Shi X, Rienstra CM
Abstract
(2)H quadrupolar line shapes deliver rich information about protein dynamics. A newly designed 3D (2)H-(13)C-(13)Csolid-state NMR magic angle spinning (MAS) experiment is presented and demonstrated on the...
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02-06-2016 03:10 PM
Site-specific analysis of heteronuclear Overhauser effects in microcrystalline proteins
Site-specific analysis of heteronuclear Overhauser effects in microcrystalline proteins
Abstract
Relaxation parameters such as longitudinal relaxation are susceptible to artifacts such as spin diffusion, and can be affected by paramagnetic impurities as e.g. oxygen, which make a quantitative interpretation difficult. We present here the site-specific measurement of 13C and 15N heteronuclear rates in an immobilized protein. For methyls, a strong effect is expected due to the three-fold rotation of the methyl group. Quantification of the 13C...
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07-03-2014 06:04 AM
[NMR paper] Site-specific identification of an a? fibril-heparin interaction site by using solid-state NMR spectroscopy.
Site-specific identification of an a? fibril-heparin interaction site by using solid-state NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Site-specific identification of an a? fibril-heparin interaction site by using solid-state NMR spectroscopy.
Angew Chem Int Ed Engl. 2012 Dec 21;51(52):13140-3
Authors: Madine J, Pandya MJ, Hicks MR, Rodger A, Yates EA, Radford SE, Middleton DA
Abstract
At the...
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06-12-2013 11:42 AM
[NMR paper] The stability of the cytochrome c scaffold as revealed by NMR spectroscopy.
The stability of the cytochrome c scaffold as revealed by NMR spectroscopy.
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J Inorg Biochem. 2004 May;98(5):814-23
Authors: Berners-Price SJ, Bertini I, Gray HB, Spyroulias GA, Turano P
NMR spectroscopy was used to study the effect of guanidinium chloride on the unfolding of horse heart and yeast iso-1 cytochrome c under mild alkaline conditions. The structural changes on the horse heart protein were detected through NOESY (Nuclear Overhauser Effect...
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11-24-2010 09:51 PM
[NMR paper] Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NM
Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR.
Biochemistry. 1997 Jan 28;36(4):699-710
Authors: Zhou H, Dahlquist FW
Bacterial chemotaxis involves autophosphorylation of a histidine kinase and transfer of the phosphoryl group to response regulators to control flagellar rotation and receptor adaptation. The...
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08-22-2010 03:31 PM
[NMR paper] Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NM
Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR.
Biochemistry. 1997 Jan 28;36(4):699-710
Authors: Zhou H, Dahlquist FW
Bacterial chemotaxis involves autophosphorylation of a histidine kinase and transfer of the phosphoryl group to response regulators to control flagellar rotation and receptor adaptation. The...
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08-22-2010 03:03 PM
[NMR paper] Site-specific N-glycosylation of human chorionic gonadotrophin--structural analysis o
Site-specific N-glycosylation of human chorionic gonadotrophin--structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy.
Related Articles Site-specific N-glycosylation of human chorionic gonadotrophin--structural analysis of glycopeptides by one- and two-dimensional 1H NMR spectroscopy.
Glycobiology. 1991 Sep;1(4):393-404
Authors: Weisshaar G, Hiyama J, Renwick AG
Glycopeptides representing individual N-glycosylation sites of the heterodimeric glycoprotein hormone human chorionic gonadotrophin (hCG) were obtained...
The anatomy of unfolding of Yfh1 is revealed by site-specific fold stability analysis measured by 2D NMR spectroscopy
Linear Mode
