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X-ray diffraction and electron microscopy data for amyloid formation of A?40 and A?42.

ABSTRACT: The data presented in this article are related to the research article entitled "One of the possible mechanisms of amyloid fibrils formation based on the sizes of primary and secondary folding nuclei of A?40 and A?42" (Dovidchenko et al., 2016) [1]. A? peptide is one of the most intensively studied amyloidogenic peptides. Despite the huge number of articles devoted to studying different fragments of A? peptide there are only several papers with correct kinetics data, also there are a few papers with X-ray data, especially for A?42. Our data present X-ray diffraction patterns both for A?40 and A?42 as well for Tris-HCl and wax. Moreover, our data provide kinetics of amyloid formation by recombinant ??40 and synthetic ??42 peptides by using electron microscopy.

SUBMITTER: Selivanova OM

PROVIDER: S-EPMC4889875 | biostudies-other | 2016 Sep

REPOSITORIES: biostudies-other

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X-ray diffraction and electron microscopy data for amyloid formation of Aβ40 and Aβ42.

Selivanova Olga M OM Grigorashvili Elizaveta I EI Suvorina Mariya Yu MY Dzhus Ulyana F UF Nikulin Alexey D AD Marchenkov Victor V VV Surin Alexey K AK Galzitskaya Oxana V OV

Data in brief 20160520

The data presented in this article are related to the research article entitled "One of the possible mechanisms of amyloid fibrils formation based on the sizes of primary and secondary folding nuclei of Aβ40 and Aβ42" (Dovidchenko et al., 2016) [1]. Aβ peptide is one of the most intensively studied amyloidogenic peptides. Despite the huge number of articles devoted to studying different fragments of Aβ peptide there are only several papers with correct kinetics data, also there are a few papers ...[more]

PMID: 27294177

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