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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Detalles Bibliográficos
Autores principales: Beveridge, Rebecca, Migas, Lukasz G., Das, Rahul K., Pappu, Rohit V., Kriwacki, Richard W., Barran, Perdita E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2019
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6488185/
https://www.ncbi.nlm.nih.gov/pubmed/30823702
http://dx.doi.org/10.1021/jacs.8b13483

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6488185/
https://www.ncbi.nlm.nih.gov/pubmed/30823702
http://dx.doi.org/10.1021/jacs.8b13483

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