Author

J. Sot

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Biophysics· 1

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Approach:mechanistic / dynamical model· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Approach:statistical model· 1

Frequent Co-Authors

C. M. Dobson· 1 shared F. Goni· 1 shared I. de la Arada· 1 shared J. D. Camino· 1 shared J. L. R. Arrondo· 1 shared N. Cremades· 1 shared P. Gracia· 1 shared S. W. Chen· 1 shared

Activity by Year

2020-2020 · peak 1/yr

Co-Author Collaboration Network

9 top collaborators · 36 mutual co-author links

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1 shared paperBiophysics

C. M. Dobson

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1 paper

Recent·Most cited

The extent of protein hydration dictates the preference for heterogeneous or homogeneous nucleation generating either parallel or antiparallel β-sheet α-synuclein aggregates

J. D. Camino, P. Gracia, S. W. Chen, J. Sot, I. de la Arada, V. Sebastian, J. L. R. Arrondo, F. Goni, C. M. Dobson, N. Cremades

This study shows that α-synuclein can form amyloid aggregates via homogeneous nucleation under limited hydration, leading to antiparallel β-sheet structures, which are more stable than parallel ones under such conditions.

bioRxiv · Sep 28, 2020Biophysics