[NMR paper] Real-Time Analysis of Folding upon Binding of a Disordered Protein by using Dissolution DNP NMR Spectroscopy.
Real-Time Analysis of Folding upon Binding of a Disordered Protein by using Dissolution DNP NMR Spectroscopy.
Related Articles Real-Time Analysis of Folding upon Binding of a Disordered Protein by using Dissolution DNP NMR Spectroscopy.
Angew Chem Int Ed Engl. 2017 May 16;:
Authors: Ragavan M, Iconaru LI, Park CG, Kriwacki RW, Hilty C
Abstract
The kinase inhibitory domain of the cell cycle regulatory protein p27(Kip1) (p27) was nuclear spin hyperpolarized using dissolution dynamic nuclear polarization (D-DNP). While...
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Identificationof Dynamic Modes in an IntrinsicallyDisordered Protein Using Temperature-Dependent NMR Relaxation
Identificationof Dynamic Modes in an IntrinsicallyDisordered Protein Using Temperature-Dependent NMR Relaxation
Anton Abyzov, Nicola Salvi, Robert Schneider, Damien Maurin, Rob W.H. Ruigrok, Malene Ringkjøbing Jensen and Martin Blackledge
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.6b02424/20160506/images/medium/ja-2016-02424a_0010.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.6b02424
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/MZI5nf_B2ds
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[NMR paper] NMR studies of protein folding and binding in cells and cell-like environments.
NMR studies of protein folding and binding in cells and cell-like environments.
NMR studies of protein folding and binding in cells and cell-like environments.
Curr Opin Struct Biol. 2014 Dec 2;30C:7-16
Authors: Smith AE, Zhang Z, Pielak GJ, Li C
Abstract
Proteins function in cells where the concentration of macromolecules can exceed 300g/L. The ways in which this crowded environment affects the physical properties of proteins remain poorly understood. We summarize recent NMR-based studies of protein folding and binding...
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NMR studies of protein folding and binding in cells and cell-like environments
NMR studies of protein folding and binding in cells and cell-like environments
Publication date: February 2015
Source:Current Opinion in Structural Biology, Volume 30</br>
Author(s): Austin E Smith , Zeting Zhang , Gary J Pielak , Conggang Li</br>
Proteins function in cells where the concentration of macromolecules can exceed 300g/L. The ways in which this crowded environment affects the physical properties of proteins remain poorly understood. We summarize recent NMR-based studies of protein folding and binding conducted in cells and in vitro under crowded...
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Bruker and Berkeley Lab Combine NMR with SAXS for Analyzing Large Protein ... - Genetic Engineering News
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Bruker and Berkeley Lab Combine NMR with SAXS for Analyzing Large Protein ...
Genetic Engineering News
Bruker and Lawrence Berkeley National Laboratory are collaborating to develop structural biology methods and tools that integrate small-angle x-ray scattering (SAXS) technology with nuclear magnetic resonance (NMR). The aim is to generate a set of data ...
Bruker and Lawrence Berkeley National Laboratory Collaborate on Novel ...MarketWatch (press release)
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11-11-2011 08:26 AM
Bruker and Berkeley Lab Combine NMR with SAXS for Analyzing Large Protein ... - Genetic Engineering News
Bruker and Berkeley Lab Combine NMR with SAXS for Analyzing Large Protein ... - Genetic Engineering News
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Bruker and Berkeley Lab Combine NMR with SAXS for Analyzing Large Protein ...
Genetic Engineering News
The aim is to generate a set of data analysis algorithms for determining the structures of larger, multi-domain proteins and protein complexes with DNA, RNA or other proteins. The organizations claim that combining the NMR-derived 3-dimensional atomic ...
Bruker and Lawrence...
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11-10-2011 08:09 PM
Engineering of a bis-chelator motif into a protein ?-helix for rigid lanthanide binding and paramagnetic NMR spectroscopy.
Engineering of a bis-chelator motif into a protein ?-helix for rigid lanthanide binding and paramagnetic NMR spectroscopy.
Engineering of a bis-chelator motif into a protein ?-helix for rigid lanthanide binding and paramagnetic NMR spectroscopy.
Chem Commun (Camb). 2011 May 27;
Authors: Swarbrick JD, Ung P, Su XC, Maleckis A, Chhabra S, Huber T, Otting G, Graham B
Attachment of two nitrilotriacetic acid-based ligands to a protein ?-helix in an i, i + 4 configuration produces an octadentate chelating motif that is able to bind paramagnetic...
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05-28-2011 06:50 PM
[NMR paper] Intestinal fatty acid binding protein: the folding mechanism as determined by NMR stu
Intestinal fatty acid binding protein: the folding mechanism as determined by NMR studies.
Related Articles Intestinal fatty acid binding protein: the folding mechanism as determined by NMR studies.
Biochemistry. 2001 Jan 23;40(3):732-42
Authors: Hodsdon ME, Frieden C
The intestinal fatty acid binding protein is composed of two beta-sheets surrounding a large interior cavity. There is a small helical domain associated with the portal for entry of the ligand into the cavity. Denaturation of the protein has been monitored in a residue-specific...
Analyzing the Folding and Binding Steps of an IntrinsicallyDisordered Protein by Protein Engineering
Linear Mode
