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Conformational dynamics of α-synuclein: insights from mass spectrometry

descriptionPublicationkeyboard_double_arrow_right Article 01 Jan 2015 United Kingdom English Publisher:Royal Society of Chemistry (RSC)Journal:The Analyst, volume 140, pages 3,070-3,081 (issn: 0003-2654, eissn: 1364-5528,

Authors: Phillips, A S; Gomes, A F; Kalapothakis, J M D; Gillam, J E; Gasparavicius, J; Gozzo, F C; Kunath, T; +2 Authors

doi: 10.1039/c4an02306d

pmid: 25756329

handle: 20.500.11820/37a4e19b-99ad-4772-90de-92a2088a1fa7

Conformational dynamics of α-synuclein: insights from mass spectrometry

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Abstract

Different mass spectrometry approaches are combined to investigate the conformational flexibility of α-synuclein.

Country

United Kingdom

Related Organizations

State University of Campinas
Brazil
University of Edinburgh
United Kingdom
University of Salford
United Kingdom
MRC Centre for Regenerative Medicine
United Kingdom
Medical Research Council
United Kingdom

Keywords

dimer formation, ligand-binding, fibril formation, Protein Conformation, metal-binding, Molecular Sequence Data, aggregation, amyloid-beta-protein, Hydrogen-Ion Concentration, Mass Spectrometry, Protein Aggregates, alpha-Synuclein, Humans, parkinsons-disease, intrinsically disordered proteins, Amino Acid Sequence, alzheimers-disease, cross-linking

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	citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).	44
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