The researchers have found a new way to design proteins in the lab such that they zip together in just the same way that DNA molecule zip up together for the double helix formation. This new technique was developed in the University of Washington School of Medicine scientists with the vision ahead that it can possibly help design proteins for nanomachines so as to potentially aid analyze and care for disease along with the permission to carry out more precise engineering of cells for performing a broad range of other tasks.
According to Zibo Chen, the machines must have precisely placed parts for better efficacy. The current method helps structure proteins that can stick together the way it is needed. The DNA has been used as a major component since the beginning in designing biomolecular nanomachines. It was a major component as the DNA strands draw closer for hydrogen bonds formation followed by the creation of DNA’s double helix; however, this happens only if the DNA sequences are complementary. The team has created a novel protein design algorithms that can develop complementary proteins which pair precisely with among each other by making use of the exact equivalent chemical language of DNA.
This groundbreaking invention assists using computational designing to produce hydrogen-bond networks for the pairing of each protein which has a unique complementary sequence. The only way to obtain this is to see that the opposite pairs do not cross-react with each other. Currently, the engineering of the cells for applications in the biotechnology or medicines such as modifying bacteria for toxic waste clean-up or developing immune cells against cancers are doing the rounds. The technique helps to understand the protein machines interaction and pave a new way for protein nanomaterial design. Researchers Iwijn De Vlaminck and his team from Cornell have pushed single-cell genomics forward by developing droplet microfluidics for revolutionizing single-cell RNA sequencing with throughput and cost-effective approach.