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In vitro perturbation of aggregation processes in β‐amyloid peptides: A spectroscopic study
Author(s) -
Sgarbossa Antonella,
Buselli Dario,
Lenci Francesco
Publication year - 2008
Publication title -
febs letters
Language(s) - Slovak
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.08.039
Subject(s) - peptide , uniprot , amyloid (mycology) , circular dichroism , chemistry , amyloid beta , biochemistry , inorganic chemistry , gene
MINT‐ 6742984 : 1‐40 beta‐amyloid peptide (uniprotkb: P05067 ) and 1‐40 beta‐amyloid peptide (uniprotkb: P05067 ) bind (MI: 0407 ) by circular dichroism (MI:0016) MINT‐ 6743002 : 1‐40 beta‐amyloid peptide (uniprotkb: P05067 ) and 1‐40 beta‐amyloid peptide (uniprotkb: P05067 ) bind (MI: 0407 ) by light scattering (MI: 0067 ) MINT‐ 6743012 : 1‐40 beta‐amyloid peptide (uniprotkb: P05067 ) and 1‐40 beta‐amyloid peptide (uniprotkb: P05067 ) bind (MI: 0407 ) by classical fluorescence spectroscopy (MI: 0017 )