SEARCH

SEARCH BY CITATION

FilenameFormatSizeDescription
cbdd12129-sup-0001-Suppmat.docxWord document2192K

Figure S1. ESI-MS recording of native Aβ12 (top) and Aβ16 (bottom) showing base peak and M/2 peak.

Figure S2. CD trace of native Aβ12 (left) and Aβ12 with Aluminium (1:1) (right). The pattern is indicative of absence of any well defined secondary structures (like random coil) in both with marginal changes in the traces.

Figure S3. Partial TOSCY of Aβ16 in phosphate buffer at 303 K.

Figure S4. Partial ROESY of Aβ16 in phosphate buffer at 303 K, showing NH-NH region (bottom) and NH – CαH region (top).

Figure S5. Overlap of natural abundance 1H – 15N HSQC spectra of free (blue) and bound (red) Aβ12 peptide in phosphate buffer at 280 K.

Figure S6. Overlap of Cα protons region of natural abundance 1H – 13C HSQC spectra of free (blue) and bound (red) Aβ12 peptide in phosphate buffer at 280 K.

Figure S7. Distribution of ϕ, ψ dihedral angles in the allowed region of Ramachandran map consisting of both free and bound forms of Aβ12.

Table S1. Total number of Metal bound protein structure involving amino acid residues present in Aβ12 fragment (number of NMR derived structures are given in brackets).

Table S2. NOEs used for CYANA structure calculation of Aβ12 peptide (free).

Please note: Wiley Blackwell is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.