Ion Mobility Mass Spectrometry Uncovers the Impact of the Patterning of Oppositely Charged Residues on the Conformational Distributions of Intrinsically Disordered Proteins

[Image: see text] The global dimensions and amplitudes of conformational fluctuations of intrinsically disordered proteins are governed, in part, by the linear segregation versus clustering of oppositely charged residues within the primary sequence. Ion mobility-mass spectrometry (IM-MS) affords uni...

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Julkaisussa:J Am Chem Soc
Päätekijät: Beveridge, Rebecca, Migas, Lukasz G., Das, Rahul K., Pappu, Rohit V., Kriwacki, Richard W., Barran, Perdita E.
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: American Chemical Society 2019
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC6488185/
https://ncbi.nlm.nih.gov/pubmed/30823702
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/jacs.8b13483
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