Transient multimers modulate conformer abundances of prion protein monomer through conformational selection
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-019-48377-w.pdf
Reference34 articles.
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2. Schor, M., Mey, A. & MacPhee, C. E. Analytical methods for structural ensembles and dynamics of intrinsically disordered proteins. Biophys Rev 8, 429–439, https://doi.org/10.1007/s12551-016-0234-6 (2016).
3. Heck, A. J. Native mass spectrometry: a bridge between interactomics and structural biology. Nat Methods 5, 927–933, https://doi.org/10.1038/nmeth.1265 (2008).
4. Han, L. & Ruotolo, B. T. Ion Mobility-Mass Spectrometry Differentiates Protein Quaternary Structures Formed in Solution and in Electrospray Droplets. Anal Chem 87, 6808–6813, https://doi.org/10.1021/acs.analchem.5b01010 (2015).
5. Uversky, V. N. & Dunker, A. K. Multiparametric analysis of intrinsically disordered proteins: looking at intrinsic disorder through compound eyes. Anal Chem 84, 2096–2104, https://doi.org/10.1021/ac203096k (2012).
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