The cold never bothered me anyway: RiAFP (LB95)

Abstract

Antifreeze proteins (AFP) exist in a wide variety of cold adapted organisms including fishes, bacteria, and insects. This unusual molecule inhibits the growth of ice crystals by irreversibly adsorbing to the flat surface of existing ice particles with a complex mechanism. The protein warps the smooth surface of ice to prevent the addition of other water molecules to the crystal, allowing the organism to survive in subzero temperatures. Longhorn beetle (Rhagium inquisitor) AFP (RiAFP) is a hyperactive protein that binds to basal, as well as prism, ice surfaces. This multiple surface attachment results in a 10‐fold higher activity than AFP in fishes. RiAFP forms a compressed [[Unsupported Character ‐ Symbol Font β]]‐solenoid architecture consisting of two parallel 6‐ and 7‐stranded [[Unsupported Character ‐ Symbol Font β]]‐sheets. Two cysteines involved in a disulfide bridge link the [[Unsupported Character ‐ Symbol Font β]]‐sandwich fold. RiAFP has an exceptionally flat and large ice‐binding surface lined with a regular array of Thr residues that are spaced at the same distance as oxygen atoms in the ice surface, creating a surface complementarity to ice. AFP are of particular interest to researchers because of their many potential uses in cryopreservation, such as tissue storage and plant genetic engineering. The Central SMART Team (Students Modeling A Research Topic) modeled RiAFP using 3D printing technology.Grant Funding Source: Supported by grants from the NIH‐SEPA and NIH‐CTSA.