[NMR paper] Segmental isotope labelling and solid-state NMR of a 12 × 59*kDa motor protein: identification of structural variability.
Segmental isotope labelling and solid-state NMR of a 12 × 59*kDa motor protein: identification of structural variability.
Related Articles Segmental isotope labelling and solid-state NMR of a 12 × 59*kDa motor protein: identification of structural variability.
J Biomol NMR. 2018 Jun 12;:
Authors: Wiegand T, Cadalbert R, von Schroetter C, Allain FH, Meier BH
Abstract
Segmental isotope labelling enables the NMR study of an individual domain within a multidomain protein, but still in the context of the entire full-length protein....
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06-28-2018 02:38 PM
[NMR paper] Protein-nucleotide contacts in motor proteins detected by DNP-enhanced solid-state NMR.
Protein-nucleotide contacts in motor proteins detected by DNP-enhanced solid-state NMR.
Related Articles Protein-nucleotide contacts in motor proteins detected by DNP-enhanced solid-state NMR.
J Biomol NMR. 2017 Nov 08;:
Authors: Wiegand T, Liao WC, Ong TC, Däpp A, Cadalbert R, Copéret C, Böckmann A, Meier BH
Abstract
DNP (dynamic nuclear polarization)-enhanced solid-state NMR is employed to directly detect protein-DNA and protein-ATP interactions and identify the residue type establishing the intermolecular contacts. While...
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11-10-2017 05:01 PM
Light microscopy provides a deep look into protein structure - Phys.org - Phys.Org
Light microscopy provides a deep look into protein structure - Phys.org - Phys.Org
http://www.bionmr.com//t2.gstatic.com/images?q=tbn:ANd9GcQG69FMdjaOzVdvO8fNDx9c1t6uv0SeGKAywKjRdVRRma0SZH4sGlq9-_q3JW8xkTHitn6biYqD
Phys.Org
<img alt="" height="1" width="1">
Light microscopy provides a deep look into protein structure - Phys.org
Phys.Org
Light microscopy continues to reveal the microscopic world at an ever increasing resolution. Using a new method coined COLD, scientists at the Max Planck ...
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01-25-2017 11:13 PM
Translocator Protein 18 kDa (TSPO): An Old Proteinwith New Functions?
Translocator Protein 18 kDa (TSPO): An Old Proteinwith New Functions?
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00142/20160509/images/medium/bi-2016-00142k_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00142
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/l_8dplFAYho
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05-10-2016 04:13 AM
Selective observation of the disordered import signal of a globular protein by in-cell NMR: The example of frataxins
Selective observation of the disordered import signal of a globular protein by in-cell NMR: The example of frataxins
Abstract
We have exploited the capability of in-cell NMR to selectively observe flexible regions within folded proteins to carry out a comparative study of two members of the highly conserved frataxin family which are found both in prokaryotes and in eukaryotes. They all contain a globular domain which shares more than 50% identity, which in eukaryotes is preceded by an N-terminal tail containing the mitochondrial import signal. We demonstrate that the NMR spectrum of...
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04-10-2015 09:46 AM
[NMR paper] Selective observation of the disordered import signal of a globular protein by in-cell NMR: The example of frataxins.
Selective observation of the disordered import signal of a globular protein by in-cell NMR: The example of frataxins.
Selective observation of the disordered import signal of a globular protein by in-cell NMR: The example of frataxins.
Protein Sci. 2015 Mar 12;
Authors: Popovic M, Sanfelice D, Pastore C, Prischi F, Temussi PA, Pastore A
Abstract
We have exploited the capability of in-cell NMR to selectively observe flexible regions within folded proteins to carry out a comparative study of two members of the highly...
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03-17-2015 05:12 PM
Selective observation of the disordered import signal of a globular protein by in-cell NMR: The example of frataxins
Selective observation of the disordered import signal of a globular protein by in-cell NMR: The example of frataxins
Abstract
We have exploited the capability of in-cell NMR to selectively observe flexible regions within folded proteins to carry out a comparative study of two members of the highly conserved frataxin family which are found both in prokaryotes and in eukaryotes. They all contain a globular domain which shares more than 50% identity, which in eukaryotes is preceded by an N-terminal tail containing the mitochondrial import signal. We demonstrate that the NMR spectrum of the...
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03-12-2015 11:38 PM
The BMRB matters
The BMRB matters
Nature Structural & Molecular Biology 19, 853 (2012) doi:10.1038/nsmb.2387
Published online 06 September 2012
NATURE STRUCTURAL & MOLECULAR BIOLOGY | EDITORIAL
http://www.nature.com/nsmb/journal/v19/n9/full/nsmb.2387.html