Crystal Structure of an Insect Antifreeze Protein and its Implications for Ice Binding
Want to listen to this article for FREE?
Complete the form below to unlock access to ALL audio articles.
Read time: Less than a minute
Background: Antifreeze proteins bind to ice crystals and inhibit their growth. Results: The crystal structure of a potent beetle antifreeze protein was determined by direct methods. Conclusion: Ordered crystallographic waters on the protein surface match several planes of hexagonal ice. Significance: The structure is the largest determined ab initio without heavy atoms and its ordered waters suggest a molecular basis for ice binding.
This article was published online in The Journal of Biological Chemistry and is free to access.
