A 3-year PhD scholarship is available from the 1 September 2015 or as soon as possible thereafter at Department of Chemistry at Technical University of Denmark and DTU Electro.
The project is funded as a part of the Danish National Research Foundation Center of Excellence Center for Hyperpolarized Magnetic Resonance:http://www.dnp.dtu.dk/
Real-time pure shift 15 N HSQC of proteins: a real improvement in resolution and sensitivity
Real-time pure shift 15 N HSQC of proteins: a real improvement in resolution and sensitivity
Abstract
Spectral resolution in proton NMR spectroscopy is reduced by the splitting of resonances into multiplets due to the effect of homonuclear scalar couplings. Although these effects are often hidden in protein NMR spectroscopy by low digital resolution and routine apodization, behind the scenes homonuclear scalar couplings increase spectral overcrowding. The possibilities for biomolecular NMR offered by new pure shift NMR methods are illustrated here....
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03-04-2015 08:56 AM
[NMR paper] Real-time protein NMR spectroscopy and investigation of assisted protein folding.
Real-time protein NMR spectroscopy and investigation of assisted protein folding.
Real-time protein NMR spectroscopy and investigation of assisted protein folding.
Biochim Biophys Acta. 2014 Dec 10;
Authors: Kumar A, Balbach J
Abstract
BACKGROUND: During protein folding reactions toward the native structure, short-lived intermediate states can be populated. Such intermediates expose hydrophobic patches and can self-associate leading to non-productive protein misfolding. A major focus of current research is the characterization...
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12-17-2014 09:43 PM
Real-time protein NMR spectroscopy and investigation of assisted protein folding
Real-time protein NMR spectroscopy and investigation of assisted protein folding
Publication date: Available online 11 December 2014
Source:Biochimica et Biophysica Acta (BBA) - General Subjects</br>
Author(s): Amit Kumar , Jochen Balbach</br>
Background During protein folding reactions toward the native structure, short-lived intermediate states can be populated. Such intermediates expose hydrophobic patches and can self-associate leading to non-productive protein misfolding. A major focus of current research is the characterization of short-lived intermediates...
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12-12-2014 11:30 AM
[NMR paper] Fast Real-Time NMR Methods for Characterizing Short-Lived Molecular States.
Fast Real-Time NMR Methods for Characterizing Short-Lived Molecular States.
Fast Real-Time NMR Methods for Characterizing Short-Lived Molecular States.
Chemphyschem. 2013 Jul 15;
Authors: Rennella E, Brutscher B
Abstract
The characterization of both the structure and the conformational dynamics of biological macromolecules, namely proteins and nucleic acids, is required for understanding the molecular mechanisms underlying physiological function and disease. Molecular dynamics involves the transient departure from the ground-state...
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07-17-2013 12:00 PM
[NMR paper] Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic eve
Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds.
Related Articles Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds.
J Am Chem Soc. 2005 Jun 8;127(22):8014-5
Authors: Schanda P, Brutscher B
We demonstrate for different protein samples that 2D 1H-15N correlation NMR spectra can be recorded in a few seconds of acquisition time using a new band-selective optimized flip-angle...
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11-25-2010 08:21 PM
Real-time NMR Studies of the Folding & Mechanisms of Protein Quality Control Machiner
Real-time NMR Studies of the Folding & Mechanisms of Protein Quality Control Machineries
* In the context of a project funded by European Research Council, two postdoctoral positions are available at the Structural Biology Institute in Grenoble (France) to study by real-time NMR the Folding & Mechanisms of Protein Quality Control (PQC) Machineries. Selected candidates will use latest NMR technologies developed at IBS to characterize self-assembly and functionally important structural rearrangements of large PQC machineries isolated at IBS.
* The laboratory host…
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