Biological Unit: Difference between revisions
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* The contacts in the biological unit differ from those in the asymmetric unit. | * The contacts in the biological unit differ from those in the asymmetric unit. | ||
<br>**The "author specified" homodimer appears unlikely in view of the | <br>**The "author specified" homodimer (in this case the same as the [[asymmetric unit]]) appears unlikely in view of the homodimer predicted by [[#Protein Interfaces, Surfaces and Assemblies Server (PISA)|PISA]] and [[#Probable Quaternary Structure Server (PQS)|PQS]], which has a much larger buried surface area. | ||
</center> | </center> | ||
Truncated proteins may form oligomers that are impossible in the native protein. For example, [[1bk5]] (karyopherin alpha) is a truncated part of the natural chain, and forms a dimer that would be prevented by the full-length chain. Dimerization is dependent upon Y397. Mutation Y397D prevents this artifactual dimerization, leading to the monomer [[1ee5]]. | Truncated proteins may form oligomers that are impossible in the native protein. For example, [[1bk5]] (karyopherin alpha) is a truncated part of the natural chain, and forms a dimer that would be prevented by the full-length chain. Dimerization is dependent upon Y397. Mutation Y397D prevents this artifactual dimerization, leading to the monomer [[1ee5]]. | ||
