[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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[ASAP] Unexpected Anomeric Acceptor Preference Observed Using dDNP NMR for Transglycosylation Studies of ß-Galactosidases
Unexpected Anomeric Acceptor Preference Observed Using dDNP NMR for Transglycosylation Studies of ß-Galactosidases
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00390/20200727/images/medium/bi0c00390_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.0c00390
http://feeds.feedburner.com/~r/acs/bichaw/~4/XvslsRGyXlY
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07-27-2020 09:21 PM
[ASAP] Structure and Catalytic Characterization of a Second Framework Al(IV) Site in Zeolite Catalysts Revealed by NMR at 35.2 T
Structure and Catalytic Characterization of a Second Framework Al(IV) Site in Zeolite Catalysts Revealed by NMR at 35.2 T
Kuizhi Chen*†, Sarah Horstmeier‡, Vy. T. Nguyen?, Bin Wang?, Steven P. Crossley?, Tram Pham?, Zhehong Gan†, Ivan Hung†, and Jeffery L. White*§
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.0c00590/20200413/images/medium/ja0c00590_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.0c00590
http://feeds.feedburner.com/~r/acs/jacsat/~4/t3FuVeVyDZo
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04-20-2020 05:10 PM
[ASAP] Pressure-Sensitive and Osmolyte-Modulated Liquid–Liquid Phase Separation of Eye-Lens ?-Crystallins
Pressure-Sensitive and Osmolyte-Modulated Liquid–Liquid Phase Separation of Eye-Lens ?-Crystallins
Süleyman Cinar, Hasan Cinar, Hue Sun Chan, Roland Winter
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.8b13636/20190423/images/medium/ja-2018-13636x_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.8b13636
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/0k8PRwEgdm4
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Molecular-Level Examination of Cu2+ Binding Structure for Amyloid Fibrils of 40-Residue Alzheimer’s ? by Solid-State NMR Spectroscopy
Molecular-Level Examination of Cu2+ Binding Structure for Amyloid Fibrils of 40-Residue Alzheimer’s ? by Solid-State NMR Spectroscopy
Sudhakar Parthasarathy, Fei Long, Yifat Miller, Yiling Xiao, Dan McElheny, Kent Thurber, Buyong Ma, Ruth Nussinov and Yoshitaka Ishii
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1072178/aop/images/medium/ja-2010-072178_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja1072178
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA ...
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02-22-2011 11:06 PM
[NMR paper] Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
Related Articles Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
J Biomol NMR. 2005 Jul;32(3):195-207
Authors: Böckmann A, Juy M, Bettler E, Emsley L, Galinier A, Penin F, Lesage A
We report site-resolved observation of hydrogen exchange in the micro-crystalline protein Crh. Our approach is based on the use of proton T2' -selective 1H-13C-13C correlation spectra for...
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12-01-2010 06:56 PM
[NMR paper] An NMR view of the folding process of a CheY mutant at the residue level.
An NMR view of the folding process of a CheY mutant at the residue level.
Related Articles An NMR view of the folding process of a CheY mutant at the residue level.
Structure. 2002 Sep;10(9):1173-1185
Authors: Garcia P, Serrano L, Rico M, Bruix M
The folding of CheY mutant F14N/V83T was studied at 75 residues by NMR. Fluorescence, NMR, and sedimentation equilibrium studies at different urea and protein concentrations reveal that the urea-induced unfolding of this CheY mutant includes an on-pathway molten globule-like intermediate that can...
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[NMR paper] Apoflavodoxin (un)folding followed at the residue level by NMR.
Apoflavodoxin (un)folding followed at the residue level by NMR.
Related Articles Apoflavodoxin (un)folding followed at the residue level by NMR.
Protein Sci. 2000 Jan;9(1):145-57
Authors: van Mierlo CP, van den Oever JM, Steensma E
The denaturant-induced (un)folding of apoflavodoxin from Azotobacter vinelandii has been followed at the residue level by NMR spectroscopy. NH groups of 21 residues of the protein could be followed in a series of 1H-15N heteronuclear single-quantum coherence spectra recorded at increasing concentrations of...