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The asymmetric unit comprises two RiAFP molecules juxtaposed with their ice-binding surfaces, however the protein is monomer in the solution.
RiAFP structure consists of β -sheets which
Two ends deviate from β helix regularity by forming capping structures.
These capping structures help to prevent end-to-end associations that would spoil the solubility of RiAFP and lead to oligomerization and aggregation.
Overall Structure
The crystallographic structure of RiAFP was defined recently[3]. It reveals a new β-solenoid architecture that forms of of remarkable regularity. The β-sheets lie on top of each other with the upper and lower strands parallel but in the opposite orientation.
Function
Disease
Relevance
Structural highlights
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The three residues in �-strand 11 at the C terminus that are too bulky to be accommodated into the core may also contribute to the capping structure to prevent amyloid-like polymerization.
Within the core there are between Thr-Ser (65-55, 85-75, 132-124 respectively) and one between Cys4-Cys21, that contributes to stabilize the whole structure.
