Prior to gene expression in the cell, the non-coding regions of the genome have to be removed by the spliceosome. A nuclear magnetic resonance (NMR) spectroscopy study by researchers in Munich suggests that distinct conformations of a member of this molecular complex play a vital role in the process, with implications for biomedical science.
Slicing the spliceosome: NMR dices protein complex - spectroscopyNOW.com
Slicing the spliceosome: NMR dices protein complex - spectroscopyNOW.com
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Slicing the spliceosome: NMR dices protein complex
spectroscopyNOW.com
Cells convert DNA to RNA to template protein production but before that final step, gene expression, the non-coding regions of the genome have to be removed by the so-called spliceosome. A nuclear magnetic resonance (NMR) spectroscopy study by ...
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12-01-2016 02:30 PM
The good, the bad and the spliceosome - Science Daily
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The good, the bad and the spliceosome
Science Daily
"By employing nuclear magnetic resonance (NMR) spectroscopy at the Bavarian NMR Center in Garching, we were able to elucidate the spatial structure of RBM5-OCRE in complex with SmN (a protein present in the spliceosome) and to understand exactly ...
The good, the bad and the spliceosome - Science Daily
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11-29-2016 09:02 PM
LXR Agonism Upregulates the Macrophage ABCA1/SyntrophinProtein Complex That Can Bind ApoA-I and Stabilized ABCA1 Protein,but Complex Loss Does Not Inhibit Lipid Efflux
LXR Agonism Upregulates the Macrophage ABCA1/SyntrophinProtein Complex That Can Bind ApoA-I and Stabilized ABCA1 Protein,but Complex Loss Does Not Inhibit Lipid Efflux
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b00894/20151109/images/medium/bi-2015-00894c_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b00894
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11-10-2015 09:10 AM
[NMR paper] Role of hydrophobic interactions in the encounter complex formation of plastocyanin and cytochrome f complex revealed by paramagnetic NMR spectroscopy.
Role of hydrophobic interactions in the encounter complex formation of plastocyanin and cytochrome f complex revealed by paramagnetic NMR spectroscopy.
Role of hydrophobic interactions in the encounter complex formation of plastocyanin and cytochrome f complex revealed by paramagnetic NMR spectroscopy.
J Am Chem Soc. 2013 Apr 29;
Authors: Scanu S, Förster J, Ullmann GM, Ubbink M
Abstract
Protein complex formation is thought to be at least a two-step process, in which the active complex is preceded by the formation of an encounter complex....
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05-01-2013 11:46 AM
NMR as a Unique Tool in Assessment and Complex Determination of Weak Protein-Protein Interactions.
NMR as a Unique Tool in Assessment and Complex Determination of Weak Protein-Protein Interactions.
NMR as a Unique Tool in Assessment and Complex Determination of Weak Protein-Protein Interactions.
Top Curr Chem. 2011 Aug 2;
Authors: Vinogradova O, Qin J
Protein-protein interactions are crucial for a wide variety of biological processes. These interactions range from high affinity (K (d) < nM) to very low affinity (K (d) > mM). While much is known about the nature of high affinity protein complexes, our knowledge about structural characteristics...
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08-03-2011 12:00 PM
Rapid identification of protein-protein interfaces for the construction of a complex model based on multiple unassigned signals by using time-sharing NMR measurements.
Rapid identification of protein-protein interfaces for the construction of a complex model based on multiple unassigned signals by using time-sharing NMR measurements.
Rapid identification of protein-protein interfaces for the construction of a complex model based on multiple unassigned signals by using time-sharing NMR measurements.
J Struct Biol. 2011 Apr 9;
Authors: Kodama Y, Reese ML, Shimba N, Ono K, Kanamori E, Dötsch V, Noguchi S, Fukunishi Y, Suzuki EI, Shimada I, Takahashi H
Protein-protein interactions are necessary for various cellular...
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04-20-2011 07:15 PM
[NMR paper] NMR techniques for identifying the interface of a larger protein-protein complex: cro
NMR techniques for identifying the interface of a larger protein-protein complex: cross-saturation and transferred cross-saturation experiments.
Related Articles NMR techniques for identifying the interface of a larger protein-protein complex: cross-saturation and transferred cross-saturation experiments.
Methods Enzymol. 2005;394:483-506
Authors: Shimada I
NMR provides detailed structural information for protein complexes with molecular weights up to 30 kDa. However, it is difficult to obtain such information on larger proteins using NMR. To...
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11-24-2010 11:14 PM
[NMR paper] NMR structure and dynamics of an RNA motif common to the spliceosome branch-point hel
NMR structure and dynamics of an RNA motif common to the spliceosome branch-point helix and the RNA-binding site for phage GA coat protein.
Related Articles NMR structure and dynamics of an RNA motif common to the spliceosome branch-point helix and the RNA-binding site for phage GA coat protein.
Biochemistry. 1998 Sep 29;37(39):13486-98
Authors: Smith JS, Nikonowicz EP
The RNA molecules that make up the spliceosome branch-point helix and the binding site for phage GA coat protein share a secondary structure motif in which two consecutive...
Slicing the spliceosome: NMR dices protein complex
Prior to gene expression in the cell, the non-coding regions of the genome have to be removed by the spliceosome. A nuclear magnetic resonance (NMR) spectroscopy study by researchers in Munich suggests that distinct conformations of a member of this molecular complex play a vital role in the process, with implications for biomedical science.
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