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J. D. Camino

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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

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

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C. M. Dobson

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Recent·Most cited

BiophysicsbioRxivSep 28, 2020

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…·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.

DOI 10.1039/d0sc05297c

protein structurestatistical model

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