RiAFP: Difference between revisions
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== Function == | == Function == | ||
RiAFP, like other AFPs, adsorb to the surface of ice crystals and lower the temperature at which these crystals grow. Consequently, creating a difference between the melting point and the freezing point known as thermal hysteresis (TH), within which the ice growth is arrested<ref>DOI 10. | RiAFP, like other AFPs, adsorb to the surface of ice crystals and lower the temperature at which these crystals grow. Consequently, creating a difference between the melting point and the freezing point known as thermal hysteresis (TH), within which the ice growth is arrested<ref>DOI 10.1098/rsif.2014.0526</ref>. | ||
== Overall Structure == | == Overall Structure == | ||
The crystallographic structure of RiAFP was defined recently<ref>DOI 10.1074/jbc.M113.450973</ref>. RiAFP has a novel β-solenoid architecture that forms <scene name='60/607864/Beta_sheets/1'>β-sandwich</scene>. This sandwich is composed of two parallel remarkably regular <scene name='60/607864/Beta_sheets_colored/1'> 6 and 7 stranded-sheets</scene>. The β-sheets lie on top of each other with the upper and lower strands parallel but in the opposite orientation. Two ends deviate from β helix regularity by forming <scene name='60/607864/Beta_sheets_capping/2'>capping structures</scene>. These capping structures help to prevent end-to-end associations that would spoil the solubility of RiAFP and lead to oligomerization and aggregation. | The crystallographic structure of RiAFP was defined recently<ref>DOI 10.1074/jbc.M113.450973</ref>. RiAFP has a novel β-solenoid architecture that forms <scene name='60/607864/Beta_sheets/1'>β-sandwich</scene>. This sandwich is composed of two parallel remarkably regular <scene name='60/607864/Beta_sheets_colored/1'> 6 and 7 stranded-sheets</scene>. The β-sheets lie on top of each other with the upper and lower strands parallel but in the opposite orientation. Two ends deviate from β helix regularity by forming <scene name='60/607864/Beta_sheets_capping/2'>capping structures</scene>. These capping structures help to prevent end-to-end associations that would spoil the solubility of RiAFP and lead to oligomerization and aggregation. | ||
