[NMR paper] NMR supersequences with real-time homonuclear broadband decoupling: Sequential acquisition of protein and small molecule spectra in a single experiment
NMR supersequences with real-time homonuclear broadband decoupling: Sequential acquisition of protein and small molecule spectra in a single experiment
NOAH (NMR byOrderedAcquisition using 1H-detection) type of pure shift NMR pulse scheme has been designed for the efficient utilization of magnetization that presents in a spin-system under consideration. The proposed strategy, PROSMASH-HSQC2 (PROtein-HSQC and SMAll molecule-HSQC Signals with Homodecoupling) uses the real-time BIRD pure shift NMR strategy and two HSQC spectra (13C-HSQC for small molecules and 15N-HSQC for 15N-isotopic labelled proteins) can be recorded in a single NMR experiment. Thus, this method permits precise determination of drug-protein interactions at atomic levels by monitoring the chemical shift perturbations, and will have potential applications in drug discovery programs.
[NMR paper] NOAH: NMR Supersequences for Small Molecule Analysis and Structure Elucidation
NOAH: NMR Supersequences for Small Molecule Analysis and Structure Elucidation
Nested NMR experiments combining up to five conventional NMR pulse sequences into one supersequence are introduced. The core 2D NMR techniques routinely employed in small molecule NMR spectroscopy, such as HSQC, HMQC, HMBC, COSY, NOESY, TOCSY, and similar, can be recorded in a single measurement. In this way the data collection time may be dramatically reduced and sample throughput increased for basic NMR applications, such as structure elucidation and verification in synthetic, medicinal, and natural product...
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08-18-2017 04:59 PM
[NMR paper] NOAH - NMR Supersequences for Small Molecule Analysis and Structure Elucidation
NOAH - NMR Supersequences for Small Molecule Analysis and Structure Elucidation
Nested NMR experiments combining up to five conventional NMR pulse sequences into one supersequence are introduced. The core two-dimensional NMR techniques routinely employed in small molecule NMR, such as HSQC, HMQC, HMBC, COSY, NOESY, TOCSY and similar, can be recorded in a single measurement dramatically reducing the data collection time and increasing sample throughput for basic NMR applications to structure elucidation and verification in synthetic, medicinal and natural product chemistry.
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06-30-2017 06:14 PM
[NMR paper] Single-Molecule Force Spectroscopy Trajectories of a Single Protein and Its Polyproteins Are Equivalent: A Direct Experimental Validation Based on A Small Protein NuG2
Single-Molecule Force Spectroscopy Trajectories of a Single Protein and Its Polyproteins Are Equivalent: A Direct Experimental Validation Based on A Small Protein NuG2
Single-molecule force spectroscopy (SMFS) has become a powerful tool in investigating the mechanical unfolding/folding of proteins at the single-molecule level. Polyproteins made of tandem identical repeats have been widely used in atomic force microscopy (AFM)-based SMFS studies, where polyproteins not only serve as fingerprints to identify single-molecule stretching events, but may also improve statistics of data...
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12-27-2016 11:04 PM
[NMR paper] A new broadband homonuclear mixing pulse for NMR with low applied power.
A new broadband homonuclear mixing pulse for NMR with low applied power.
A new broadband homonuclear mixing pulse for NMR with low applied power.
J Chem Phys. 2014 Jul 14;141(2):024201
Authors: Coote P, Leigh KE, Yu TY, Khaneja N, Wagner G, Arthanari H
Abstract
Broadband homonuclear mixing pulses with low radiofrequency power are essential for NMR spectroscopy of proteins and small molecules, especially for emerging applications in high field NMR. We have analytically designed a mixing pulse with high bandwidth-to-power ratio,...
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07-17-2014 12:17 PM
[NMR paper] Sequential protein NMR assignments in the liquid state via sequential data acquisition.
Sequential protein NMR assignments in the liquid state via sequential data acquisition.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Sequential protein NMR assignments in the liquid state via sequential data acquisition.
J Magn Reson. 2013 Dec 14;239C:23-28
Authors: Wiedemann C, Bellstedt P, Kirschstein A, Häfner S, Herbst C, Görlach M, Ramachandran R
Abstract
Two different NMR pulse schemes involving sequential (1)H data acquisition are...
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01-04-2014 01:39 AM
[NMR paper] Enhancing the resolution of multi-dimensional heteronuclear NMR spectra of intrinsically disordered proteins by homonuclear broadband decoupling.
Enhancing the resolution of multi-dimensional heteronuclear NMR spectra of intrinsically disordered proteins by homonuclear broadband decoupling.
Related Articles Enhancing the resolution of multi-dimensional heteronuclear NMR spectra of intrinsically disordered proteins by homonuclear broadband decoupling.
Chem Commun (Camb). 2013 Dec 23;
Authors: Helge Meyer N, Zangger K
Abstract
Limited spectral resolution in the proton dimension of NMR spectra is a severe problem in intrinsically disordered proteins. Here we show that homonuclear...
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12-25-2013 03:39 PM
[NMR paper] Sequential protein NMR assignments in the liquid state via sequential data acquisition
Sequential protein NMR assignments in the liquid state via sequential data acquisition
Publication date: Available online 14 December 2013
Source:Journal of Magnetic Resonance</br>
Author(s): Christoph Wiedemann , Peter Bellstedt , Anika Kirschstein , Sabine Häfner , Christian Herbst , Matthias Görlach , Ramadurai Ramachandran</br>
Two different NMR pulse schemes involving sequential 1H data acquisition are presented for achieving protein backbone sequential resonance assignments: (i) acquisition of 3D {HCCNH & HNCACONH} and (ii) collection of 3D {HNCOCANH &...
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12-14-2013 04:48 PM
[Question from NMRWiki Q&A forum] About paragnetic impurities, inorganic salts, bad workups, etc. and their impact on small-molecule NMR spectra
About paragnetic impurities, inorganic salts, bad workups, etc. and their impact on small-molecule NMR spectra
I sometimes face the challenge of explaining to my organic chemists that, even if no impurity signals are visible in their 1H spectrum, other signs (like FID shape, very poor s/n compared to what could be expected with the sample qty, broad peaks, bad resolution...) indicate that clearly, something is wrong with their sample.
Everybody would agree that it's way much easier to convince an invidual based on concrete facts ("look, here we can see solvent/starting material/side...
NMR supersequences with real-time homonuclear broadband decoupling: Sequential acquisition of protein and small molecule spectra in a single experiment
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