ArticleEuropean biophysics journal : EBJ2008
Solution NMR and CD spectroscopy of an intrinsically disordered, peripheral membrane protein: evaluation of aqueous and membrane-mimetic solvent conditions for studying the conformational adaptability of the 18.5 kDa isoform of myelin basic protein (MBP).
Article in European biophysics journal : EBJ, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Secondary structural analysis of the carboxyl-terminal domain from different connexin isoforms.Biopolymers · 2016Article
- The proline-rich region of 18.5 kDa myelin basic protein binds to the SH3-domain of Fyn tyrosine kinase with the aid of an upstream segment to form a dynamic complex in vitro.Bioscience reports · 2014Article
- ¹H, ¹³C, and ¹⁵N backbone resonance assignments of the connexin43 carboxyl terminal domain attached to the 4th transmembrane domain in detergent micelles.Biomolecular NMR assignments · 2013Article
- Article
- Structured functional domains of myelin basic protein: cross talk between actin polymerization and Ca(2+)-dependent calmodulin interaction.Biophysical journal · 2011Article
- Charge isomers of myelin basic protein: structure and interactions with membranes, nucleotide analogues, and calmodulin.PloS one · 2011Article
- Novel strategies for drug discovery based on Intrinsically Disordered Proteins (IDPs).International journal of molecular sciences · 2011Review
- Copper uptake induces self-assembly of 18.5 kDa myelin basic protein (MBP).Biophysical journal · 2010Article
- Fuzzy complexes of myelin basic protein: NMR spectroscopic investigations of a polymorphic organizational linker of the central nervous system.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2010Review
- Optimizing the solution conditions to solve the structure of the Connexin43 carboxyl terminus attached to the 4(th) transmembrane domain in detergent micelles.Cell communication & adhesion · 2010Article
- Intrinsically disordered proteins and their environment: effects of strong denaturants, temperature, pH, counter ions, membranes, binding partners, osmolytes, and macromolecular crowding.The protein journal · 2009Review
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2 authors.
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Abstract
The stability and secondary structure propensity of recombinant murine 18.5 kDa myelin basic protein (rmMBP, 176 residues) was assessed using circular dichroic and nuclear magnetic resonance spectroscopy (1H-15N HSQC experiments) to determine the optimal sample conditions for further NMR studies (i.e., resonance assignments and protein-protein interactions). Six solvent conditions were selected based on their ability to stabilise the protein, and their tractability to currently standard solution NMR methodology. Selected solvent conditions were further characterised as functions of concentration, temperature, and pH. The results of these trials indicated that 30% TFE-d2 in H2O (v/v), pH 6.5 at 300 K, and 100 mM KCl, pH 6.5 at 277 K were the best conditions to use for future solution NMR studies of MBP. Micelles of DPC were found to be inappropriate for backbone resonance assignments of rmMBP in this instance.
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18449534What OpenQuestion holds
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