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1) and are also consistent, as expected, with secondary structure predictions (Fig. Figure 1 shows the most favoured model returned by QUARK (a) alongside representatives of the largest clusters from the ROSETTA runs (b and c). Terminal regions vary somewhat in conformation but the central portion from residues 21–35 consistently folds into a β-hairpin.

This hairpin is also present in all the returned QUARK models, as well as smaller, less-favoured clusters of structures from ROSETTA modelling despite differences in terminal regions and is therefore a strongly predicted feature of the models.

We have previously suggested that a similar β -hairpin may be present in insoluble medin fibrils.

Medin models generated online using QUARK (a) and locally in two runs of ROSETTA including (b) or excluding (c) fragments deriving from structures of lactadherin C2 domain and homologues (NHC). Secondary structure assignment was performed using DSSPThe results of all three modelling efforts agree to a remarkable degree (Fig.Short peptides composed only of these eight residues are capable of rapid aggregation into microcrystalline fibres.It is essential to identify and understand the interactions that occur early in the aggregation process that result in formation of amyloid fibrils.Due to the highly dynamic and often rapid aggregation kinetics of amyloid proteins, obtaining structural information about the soluble early stages of aggregation presents a considerable challenge.In this study we employed a variety of measures to obtain the first structural information about medin in its soluble form.

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