Michael Blaber, Ph.D. in FSU’s College of Medicine recently published his manuscript in the Journal of Proteins and Proteomics. This article, titled “Evaluation of steric entanglement in coiled-coil and domain-swapped protein interfaces using 3D printed models,” looks at protein models in a new way. These models could not previously be studied because the technology did not yet exist. Blaber references Crick’s proposed model called “Knobs in Holes” which has since been modified.

Blaber continues this research with his new findings from 3D models. He originally used a filament called Standard Polly-lactic Acid (PLA), but found it to be too brittle for his models. Because of this he switched to thermoplastic urethane filament (TPU). This switch allowed Blaber to analyze the models and determine they provide little evidence for steric entanglement of the interface.

The results showed that measurable entanglement was only found in antiparallel coiled-coils which are not as common as parallel coiled-coils. Blaber anticipated the greatest amount of entanglement in the wild-type Monofoil definition of N- and C-termini. However, he found that this definition had the least entanglement of his 3D models. This new data suggests that such entanglement is likely to not be selected in protein evolution.

Though Blaber’s results contradicted previous research findings, a more recent study by Tenorio et al. (2020) reported similar findings to Blaber’s study. His research expands on current knowledge of the amount of entanglement present in various types of coiled-coil proteins.

We congratulate Michael Blaber on his publication and his scientific contribution! To read the full manuscript visit https://link.springer.com/article/10.1007/s42485-022-00099-w#Sec3.