1inb

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

A MODEL OF THE THREE-DIMENSIONAL STRUCTURE OF ICE NUCLEATION PROTEINS

spinqualitylabelsall models 1inb Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum Publication Abstract from PubMed Bacterial ice-nucleation proteins are among the most active natural ice nucleants and can reduce the supercooling point of water in plants, thereby reducing the ability of sensitive plants to avoid damaging ice formation. We describe a structural model for bacterial ice-nucleation proteins based on molecular modelling. This model predicts a largely planar extended molecule, with one side serving as a template for orienting water into an ice lattice and the other side interacting with the membrane. The model also predicts that single molecules can form aggregates of unlimited size by interdigitation. A model of the three-dimensional structure of ice nucleation proteins.,Kajava AV, Lindow SE J Mol Biol. 1993 Aug 5;232(3):709-17. PMID:8355267 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA