Data in Brief
(Feb 2017)
Assignment of polymorphic species of insulin analogues in ion mobility mass spectroscopy
Maely P. Fávero-Retto,
Luiz Henrique Guerreiro,
Cássio M. Pessanha,
Leonardo C. Palmieri,
Luís Maurício T.R. Lima
Affiliations
Maely P. Fávero-Retto
Federal University of Rio de Janeiro – UFRJ, Av. Carlos Chagas Filho 373, CCS, Bss24, Ilha do Fundão, 21941-590 Rio de Janeiro, RJ, Brazil
Luiz Henrique Guerreiro
Federal University of Rio de Janeiro – UFRJ, Av. Carlos Chagas Filho 373, CCS, Bss24, Ilha do Fundão, 21941-590 Rio de Janeiro, RJ, Brazil
Cássio M. Pessanha
Federal University of Rio de Janeiro – UFRJ, Av. Carlos Chagas Filho 373, CCS, Bss24, Ilha do Fundão, 21941-590 Rio de Janeiro, RJ, Brazil
Leonardo C. Palmieri
Federal University of Rio de Janeiro – UFRJ, Av. Carlos Chagas Filho 373, CCS, Bss24, Ilha do Fundão, 21941-590 Rio de Janeiro, RJ, Brazil
Luís Maurício T.R. Lima
Federal University of Rio de Janeiro – UFRJ, Av. Carlos Chagas Filho 373, CCS, Bss24, Ilha do Fundão, 21941-590 Rio de Janeiro, RJ, Brazil
DOI
https://doi.org/10.1016/j.dib.2016.12.020
Journal volume & issue
Vol. 10,
no. C
Abstract
Read online
Electrospray ionization – ion mobility spectrometry – mass spectrometry (ESI–IMS–MS) allows the identification of protein polymorphic distribution of protein conformers and oligomers. We report the detailed identification of the species observed with commercially available pharmaceutical preparation of wild-type, regular human insulin.
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