Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Angew Chem Int Ed Engl. 2011 Sep 16;
Authors: Schanda P, Huber M, Boisbouvier J, Meier BH, Ernst M
PMID: 21928443
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09-20-2011 03:10 PM
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.
Angew Chem Int Ed Engl. 2011 Sep 14;
Authors: Schanda P, Huber M, Boisbouvier J, Meier BH, Ernst M
PMID: 21915969
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09-15-2011 08:31 PM
Accurate measurement of one-bond H-X heteronuclear dipolar couplings in MAS solid-state NMR.
Accurate measurement of one-bond H-X heteronuclear dipolar couplings in MAS solid-state NMR.
Accurate measurement of one-bond H-X heteronuclear dipolar couplings in MAS solid-state NMR.
J Magn Reson. 2011 Mar 21;
Authors: Schanda P, Meier BH, Ernst M
The accurate experimental determination of dipolar-coupling constants for one-bond heteronuclear dipolar couplings in solids is a key for the quantification of the amplitudes of motional processes. Averaging of the dipolar coupling reports on motions on time scales up to the inverse of the coupling...
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04-13-2011 11:57 PM
Accurate Measurement of One-Bond H-X Heteronuclear Dipolar Couplings in MAS Solid-State NMR
Accurate Measurement of One-Bond H-X Heteronuclear Dipolar Couplings in MAS Solid-State NMR
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 21 March 2011</br>
Paul, Schanda , Beat H., Meier , Matthias, Ernst</br>
The accurate experimental determination of dipolar-coupling constants for one-bond heteronuclear dipolar couplings in solids is a key for the quantification of the amplitudes of motional processes. Averaging of the dipolar coupling reports on motions on time scales up to the inverse of the coupling constant, in...
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03-22-2011 07:30 AM
Solid-state NMR detection of (14) N?(13) C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Solid-state NMR detection of (14) N?(13) C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Solid-state NMR detection of (14) N?(13) C dipolar couplings between amino acid side groups provides constraints on amyloid fibril architecture.
Magn Reson Chem. 2011 Feb;49(2):65-9
Authors: Middleton DA
Solid-state nuclear magnetic resonance (SSNMR) is a powerful technique for the structural analysis of amyloid fibrils. With suitable isotope labelling patterns, SSNMR can provide constraints on the...
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01-22-2011 01:52 PM
Solid-State NMR Studies of Amyloid Fibril Structure.
Solid-State NMR Studies of Amyloid Fibril Structure.
Solid-State NMR Studies of Amyloid Fibril Structure.
Annu Rev Phys Chem. 2010 Apr 2;
Authors: Tycko R
Current interest in amyloid fibrils stems from their involvement in neurodegenerative and other diseases and from their role as an alternative structural state for many peptides and proteins. Solid-state nuclear magnetic resonance (NMR) methods have the unique capability of providing detailed structural constraints for amyloid fibrils, sufficient for the development of full molecular models. In...
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01-12-2011 11:11 AM
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
J Am Chem Soc. 2010 Dec 27;
Authors: Esadze A, Li DW, Wang T, Bru?schweiler R, Iwahara J
Despite their importance in macromolecular interactions and functions, the dynamics of lysine side-chain amino groups in proteins are not well understood. In this study, we have developed the methodology for the investigations of the dynamics...
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12-29-2010 04:04 PM
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear 1H-15N NMR Spectroscopy
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear 1H-15N NMR Spectroscopy
Alexandre Esadze, Da-Wei Li, Tianzhi Wang, Rafael Bru?schweiler and Junji Iwahara
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja107847d/aop/images/medium/ja-2010-07847d_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja107847d
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/iFwgRBt-zto