On the basis of the collision cross section data ( Fig.4 ) for YGGFL, NNQQNY, VEALYL and SSTNVG we conclude that highly significant differences are observed in the soluble self-assembly phase of all peptides, but especially between the fibril (NNQQNY, VEALYL and SSTNVG) and the crystal lattice forming (YGGFL) classes of peptides.
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Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to β-sheet in amyloid fibril formation.
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