RMSF statistics for 300 K trajectories (Å)^a.

	Pt-Aβ16	Pt-Aβ42
Mean	3.61	7.49
SD	1.03	1.77
Min	2.32	4.41
Max	6.06	12.66

^aC_α–C_α distances in Pt-Aβ16 and Pt-Aβ42 are used to interrogate the tertiary structure of the peptides, as represented in the contact maps in Fig. 2. In the shorter peptide, the longest inter-residue distances occur for Asp1, with values in excess of 20 Å for residues Val12 through Lys16. Indeed there is little structure in the contact map: close contact between Pt-binding residues 6 and 14 is apparent, while the sequence between these is also restricted to relatively short distances. The longer peptide exhibits more structure: Asp1 again has the longest distances, most notably to amino acids in the CHC and the extreme C-terminus. Longer distances are also found for the sequences Ser8-Tyr10 with Asp23-Lys28. Short contact is found for His6 with His14 and the residues between them, and also between Phe19-Ala21 with Gly29-Gly33.