[NMR paper] Comparative Assessment of NMR Probes for the Experimental Description of Protein Folding Pathways with High-Pressure NMR
Comparative Assessment of NMR Probes for the Experimental Description of Protein Folding Pathways with High-Pressure NMR
Multidimensional NMR intrinsically provides multiple probes that can be used for deciphering the folding pathways of proteins: NH amide and C?H? groups are strategically located on the backbone of the protein, while CH(3) groups, on the side-chain of methylated residues, are involved in important stabilizing interactions in the hydrophobic core. Combined with high hydrostatic pressure, these observables provide a powerful tool to explore the conformational landscapes of...
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[NMR paper] NMR Spectroscopy of Soluble Protein Complexes at One Mega-Dalton and Beyond.
NMR Spectroscopy of Soluble Protein Complexes at One Mega-Dalton and Beyond.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles NMR Spectroscopy of Soluble Protein Complexes at One Mega-Dalton and Beyond.
Angew Chem Int Ed Engl. 2013 Jul 19;
Authors: Mainz A, Religa TL, Sprangers R, Linser R, Kay LE, Reif B
Abstract
Bigger is better: Sequential backbone assignments are obtained by NMR spectroscopy for a 1 MDa proteasome...
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[NMR paper] Protein folding and stability investigated by fluorescence, circular dichroism (CD),
Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story.
Related Articles Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story.
J Biotechnol. 2000 May 26;79(3):281-98
Authors: van Mierlo CP, Steensma E
In this review, the experimental results obtained on the folding and stability of Azotobacter vinelandii flavodoxin are summarised. By doing...