The North Atlantic Ocean is a cold, inhospitable, and often ice-covered place. In spite of these harsh conditions, life continues to thrive in the cold, dark depths. The vast majority of these winter-resident species owe their success to various forms of anti-freeze proteins. Within Northern Atlantic resident species, there are six classes of Anti-Freeze Proteins (AFPs), generally categorized by molecular size, structure and effectiveness. AFPs are a remarkable exhibition of convergent evolution – there are vast multitudes of AFPs, all present in species with no significant common ancestry. Additionally, there is no ‘common ancestry’ in the proteins themselves; some are fibrous, some are globular, some are orders of magnitude larger than others. The sheer number of individual solutions to the issue of freezing is remarkable – all AFPs perform the same role, that of preventing freezing.
Anti-Freeze Proteins generally do not function like traditional industrial solutions for freezing – they do not lower the temperature at which water freezes. Technically, AFPs do not prevent freezing at all – rather, they prevent the formation of large ice crystals. This is achieved by binding the protein to the surface of small ice crystals through …show more content…
It is also found in the frigid North Atlantic, and utilizes the Anti-Freezing Protein 1WFB. This scleroprotein is fibrous, and consists of 38 amino acids after removal of the initial signal peptide, as well as a secondary sacrificial section. Before cleaving, the full chain is 82 amino acids long. As the initial form is only present during the production of the protein, it will not be investigated in depth. Secondary structure in the 1WFB protein is peculiar – it contains no regular helices. Rather, it consists of one Coil which does not fit any specific helix classification. This coil encompasses the entire length of the protein except the final position
Anti-Freeze Proteins generally do not function like traditional industrial solutions for freezing – they do not lower the temperature at which water freezes. Technically, AFPs do not prevent freezing at all – rather, they prevent the formation of large ice crystals. This is achieved by binding the protein to the surface of small ice crystals through …show more content…
It is also found in the frigid North Atlantic, and utilizes the Anti-Freezing Protein 1WFB. This scleroprotein is fibrous, and consists of 38 amino acids after removal of the initial signal peptide, as well as a secondary sacrificial section. Before cleaving, the full chain is 82 amino acids long. As the initial form is only present during the production of the protein, it will not be investigated in depth. Secondary structure in the 1WFB protein is peculiar – it contains no regular helices. Rather, it consists of one Coil which does not fit any specific helix classification. This coil encompasses the entire length of the protein except the final position