[NMR paper] Proton-clouds to measure long-range contacts between non-exchangeable sidechain protons in solid-state NMR.
Proton-clouds to measure long-range contacts between non-exchangeable sidechain protons in solid-state NMR.
Related Articles Proton-clouds to measure long-range contacts between non-exchangeable sidechain protons in solid-state NMR.
J Am Chem Soc. 2014 Jan 27;
Authors: Sinnige T, Daniels M, Baldus M, Weingarth M
Abstract
We show that selective labeling of proteins with protonated amino acids embedded in a perdeuterated matrix, dubbed 'proton clouds', provides general access to long-range contacts between non-exchangeable sidechain protons...
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01-29-2014 02:01 PM
A Simple Method to Measure Protein Side-Chain MobilityUsing NMR Chemical Shifts
A Simple Method to Measure Protein Side-Chain MobilityUsing NMR Chemical Shifts
Mark V. Berjanskii and David S. Wishart
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja407509z/aop/images/medium/ja-2013-07509z_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja407509z
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/qRQjRZhXxAM
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09-23-2013 09:41 PM
[NMR paper] A simple method to measure protein side-chain mobility using NMR chemical shifts.
A simple method to measure protein side-chain mobility using NMR chemical shifts.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles A simple method to measure protein side-chain mobility using NMR chemical shifts.
J Am Chem Soc. 2013 Sep 13;
Authors: Berjanskii MV, Wishart DS
Abstract
Protein side-chain motions are involved in many important biological processes including enzymatic catalysis, allosteric regulation, and the mediation of protein-protein,...
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09-17-2013 11:36 PM
Side-chain to backbone correlations from solid-state NMR of perdeuterated proteins through combined excitation and long-range magnetization transfers
Side-chain to backbone correlations from solid-state NMR of perdeuterated proteins through combined excitation and long-range magnetization transfers
Abstract Proteins with excessive deuteration give access to proton detected solid-state NMR spectra of extraordinary resolution and sensitivity. The high spectral quality achieved after partial proton back-exchange has been shown to start a new era for backbone assignment, protein structure elucidation, characterization of protein dynamics, and access to protein parts undergoing motion. The large absence of protons at non-exchangeable...
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08-11-2011 02:24 AM
Side-chain to backbone correlations from solid-state NMR of perdeuterated proteins through combined excitation and long-range magnetization transfers.
Side-chain to backbone correlations from solid-state NMR of perdeuterated proteins through combined excitation and long-range magnetization transfers.
Side-chain to backbone correlations from solid-state NMR of perdeuterated proteins through combined excitation and long-range magnetization transfers.
J Biomol NMR. 2011 Aug 7;
Authors: Linser R
Proteins with excessive deuteration give access to proton detected solid-state NMR spectra of extraordinary resolution and sensitivity. The high spectral quality achieved after partial proton back-exchange...
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08-09-2011 12:11 PM
Structure Calculation from Unambiguous Long-Range Amide and Methyl (1)H-(1)H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy.
Structure Calculation from Unambiguous Long-Range Amide and Methyl (1)H-(1)H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy.
Structure Calculation from Unambiguous Long-Range Amide and Methyl (1)H-(1)H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy.
J Am Chem Soc. 2011 Mar 24;
Authors: Linser R, Bardiaux B, Higman V, Fink U, Reif B
Magic-angle spinning (MAS) solid-state NMR becomes an increasingly important tool for the determination of structures of membrane...
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03-26-2011 07:00 PM
Structure Calculation from Unambiguous Long-Range Amide and Methyl 1H-1H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy
Structure Calculation from Unambiguous Long-Range Amide and Methyl 1H-1H Distance Restraints for a Microcrystalline Protein with MAS Solid-State NMR Spectroscopy
Rasmus Linser, Benjamin Bardiaux, Victoria Higman, Uwe Fink and Bernd Reif
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja110222h/aop/images/medium/ja-2010-10222h_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja110222h
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http://feeds.feedburner.com/~r/acs/jacsat/~4/Dh0EBf8PwcY
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03-24-2011 08:02 PM
Optimum levels of exchangeable protons in perdeuterated proteins for proton detection in MAS solid-state NMR spectroscopy
Optimum levels of exchangeable protons in perdeuterated proteins for proton detection in MAS solid-state NMR spectroscopy
Abstract We present a systematic study of the effect of the level of exchangeable protons on the observed amide proton linewidth obtained in perdeuterated proteins. Decreasing the amount of D2O employed in the crystallization buffer from 90 to 0%, we observe a fourfold increase in linewidth for both 1H and 15N resonances. At the same time, we find a gradual increase in the signal-to-noise ratio (SNR) for 1Hâ??15N correlations in dipolar coupling based experiments for...
Proton Clouds to Measure Long-Range Contacts between Nonexchangeable Side Chain Protons in Solid-State NMR
Linear Mode
