Venkat Reddy Chirasani’s favorite structure is:

Crystal structure of the hyperactive Type I antifreeze from winter flounder

AFP

Why?

Generally a polypeptide chain folds into a protein by hiding hydrophobic residues in its core by expelling water from its core. But this recently crystallized anti-freeze protein has retained ~400 water molecules in its core.  This dimeric, four-helix bundle protein has putative ice-binding residues. These residues point inwards and coordinate the interior waters into two intersecting polypentagonal networks. The inter helical contacts are minimal but the bundle is stabilized by anchoring the protein's backbone carbonyl groups to semi-clathrate water monolayers. The ordered waters likely involve in ice binding by extending outwards to the protein surface. Thus, this protein fold supports both the mechanisms of expelling water from the core of the protein for proper protein folding and the adsorption of antifreeze protein through anchored-clathrate water.—Venkat Reddy Chirasani

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