RiAFP: Difference between revisions
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
The asymmetric unit comprises two RiAFP molecules juxtaposed with their ice-binding surfaces, however the protein is monomer in the solution. | |||
β-solenoid architecture. | |||
β -sandwich of two parallel 6 and 7 stranded-sheets of remarkable regularity. | |||
RiAFP structure consists of β -sheets which 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 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<ref>DOI 10.1074/jbc.M113.450973</ref>. | |||
== Function == | == Function == | ||
<scene name='60/607864/Riafp/1'>TextToBeDisplayed</scene> | <scene name='60/607864/Riafp/1'>TextToBeDisplayed</scene> | ||
