[ASAP] Exposing the Interplay Between Enzyme Turnover, Protein Dynamics, and the Membrane Environment in Monoamine Oxidase B
Exposing the Interplay Between Enzyme Turnover, Protein Dynamics, and the Membrane Environment in Monoamine Oxidase B
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.9b00213/20190423/images/medium/bi-2019-00213b_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.9b00213
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04-23-2019 07:54 PM
Analyzing protein structures in their native environment - MIT News
Analyzing protein structures in their native environment - MIT News
Analyzing protein structures in their native environment MIT NewsProteins can fold in different ways depending on their environment. These different configurations change the function of the protein; misfolding is frequently ...
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01-07-2019 05:49 AM
[NMR paper] A strategy for co-translational folding studies of ribosome-bound nascent chain complexes using NMR spectroscopy.
A strategy for co-translational folding studies of ribosome-bound nascent chain complexes using NMR spectroscopy.
Related Articles A strategy for co-translational folding studies of ribosome-bound nascent chain complexes using NMR spectroscopy.
Nat Protoc. 2016 Aug;11(8):1492-1507
Authors: Cassaignau AM, Launay HM, Karyadi ME, Wang X, Waudby CA, Deckert A, Robertson AL, Christodoulou J, Cabrita LD
Abstract
During biosynthesis on the ribosome, an elongating nascent polypeptide chain can begin to fold, in a process that is central...
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07-29-2016 03:01 PM
Analyzing protein structures in their native environment - MIT News
Analyzing protein structures in their native environment - MIT News
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Analyzing protein structures in their native environment
MIT News
Until now, it has been difficult to fully characterize the different structures that proteins can take on in their natural environments. However, using a new technique known as sensitivity-enhanced nuclear magnetic resonance (NMR), MIT researchers have ...
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11-22-2015 01:36 AM
[NMR paper] Increasing the sensitivity of NMR diffusion measurements by paramagnetic longitudinal relaxation enhancement, with application to ribosome-nascent chain complexes.
Increasing the sensitivity of NMR diffusion measurements by paramagnetic longitudinal relaxation enhancement, with application to ribosome-nascent chain complexes.
Related Articles Increasing the sensitivity of NMR diffusion measurements by paramagnetic longitudinal relaxation enhancement, with application to ribosome-nascent chain complexes.
J Biomol NMR. 2015 Aug 8;
Authors: Chan SH, Waudby CA, Cassaignau AM, Cabrita LD, Christodoulou J
Abstract
The translational diffusion of macromolecules can be examined non-invasively by...
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08-09-2015 05:01 PM
Increasing the sensitivity of NMR diffusion measurements by paramagnetic longitudinal relaxation enhancement, with application to ribosomeâ??nascent chain complexes
Increasing the sensitivity of NMR diffusion measurements by paramagnetic longitudinal relaxation enhancement, with application to ribosomeâ??nascent chain complexes
Abstract
The translational diffusion of macromolecules can be examined non-invasively by stimulated echo (STE) NMR experiments to accurately determine their molecular sizes. These measurements can be important probes of intermolecular interactions and protein folding and unfolding, and are crucial in monitoring the integrity of large macromolecular assemblies...
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08-08-2015 12:17 PM
[NMR paper] Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy.
Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy.
Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy.
Acc Chem Res. 2013 Jul 5;
Authors: Opella SJ
Abstract
One of the most important topics in experimental structural biology is determining the structures of membrane proteins. These structures represent one-third of all of the information...