[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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Segmental isotope labelling and solid-state NMR of a 12â??Ã?â??59Â*kDa motor protein: identification of structural variability
Segmental isotope labelling and solid-state NMR of a 12â??Ã?â??59Â*kDa motor protein: identification of structural variability
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. Compared to the fully labelled protein, spectral overlap can be greatly reduced. We here describe segmental labelling of the (double-) hexameric DnaB helicase from Helicobacter pylori using a ligation approach. Solid-state spectra demonstrate that the...
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[NMR paper] A new strategy for sequential assignment of intrinsically unstructured proteins based on 15N single isotope labelling
A new strategy for sequential assignment of intrinsically unstructured proteins based on 15N single isotope labelling
Publication date: Available online 23 July 2013
Source:Journal of Magnetic Resonance</br>
Author(s): Juan Lopez , Puneet Ahuja , Melanie Gérard , Jean Michel Wieruszeski , Guy Lippens</br>
We describe a new efficient strategy for the sequential assignment of amide resonances of a conventional 15N-1H HSQC spectrum of intrinsically unfolded proteins, based on composite NOESY-TOCSY and TOCSY-NOESY mixing times. These composite mixing times lead to a...
Suppression of isotope scrambling in cell-free protein synthesis by broadband inhibition of PLP enymes for selective 15N-labelling and production of perdeuterated proteins in H2O
Suppression of isotope scrambling in cell-free protein synthesis by broadband inhibition of PLP enymes for selective 15N-labelling and production of perdeuterated proteins in H2O
Abstract Selectively isotope labelled protein samples can be prepared in vivo or in vitro from selectively labelled amino acids but, in many cases, metabolic conversions between different amino acids result in isotope scrambling. The best results are obtained by cell-free protein synthesis, where metabolic enzymes are generally less active, but isotope scrambling can never be suppressed completely. We show that...
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02-16-2011 09:34 PM
Cell-free expression and stable isotope labelling strategies for membrane proteins
Cell-free expression and stable isotope labelling strategies for membrane proteins
Abstract Membrane proteins are highly underrepresented in the structural data-base and remain one of the most challenging targets for functional and structural elucidation. Their roles in transport and cellular communication, furthermore, often make over-expression toxic to their host, and their hydrophobicity and structural complexity make isolation and reconstitution a complicated task, especially in cases where proteins are targeted to inclusion bodies. The development of cell-free expression systems...
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01-09-2011 12:46 PM
[NMR paper] Amino acid type selective isotope labelling of the multidrug ABC transporter LmrA for
Amino acid type selective isotope labelling of the multidrug ABC transporter LmrA for solid-state NMR studies.
Related Articles Amino acid type selective isotope labelling of the multidrug ABC transporter LmrA for solid-state NMR studies.
FEBS Lett. 2004 Jun 18;568(1-3):117-21
Authors: Mason AJ, Siarheyeva A, Haase W, Lorch M, van Veen H, Glaubitz C
The ABC transporter LmrA in Lactococcus lactis confers resistance to a wide range of antibiotics and cytotoxic drugs and is a functional homologue of P-glycoprotein. Recently, solid-state NMR...
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11-24-2010 09:51 PM
[NMR paper] Biosynthetic 15N and 13C isotope labelling of glutathione in the mixed disulfide with
Biosynthetic 15N and 13C isotope labelling of glutathione in the mixed disulfide with Escherichia coli glutaredoxin documented by sequence-specific NMR assignments.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Biosynthetic 15N and 13C isotope labelling of glutathione in the mixed disulfide with Escherichia coli glutaredoxin documented by sequence-specific NMR assignments.
Eur J Biochem. 1993 Dec 1;218(2):327-34
Authors: Bushweller JH,...
Optimal isotope labelling for NMR protein structure determinations - Nature.com
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