We are delighted to share that our PhD student Nayanika Das has embarked on a research visit to the laboratory of Prof. Gerard Roelfes at the University of Groningen, The Netherlands. This visit marks an exciting step forward in her doctoral work on understanding and optimizing the function of enzymes, this time for proteins containing artificial amino acids.
During her stay, Nayanika will collaborate closely with the Roelfes group to investigate the incorporation of the noncanonical amino acid para-aminophenylalanine (pAF) into the nonenzymatic protein scaffold LmrR. Remarkably, this modification transforms LmrR into a proficient and stereoselective artificial enzyme (LmrR_pAF) — an elegant example of how chemical innovation can endow proteins with entirely new catalytic functions.
Nayanika’s research will combine experimental validation in the laboratory with computational modeling efforts. Specifically, she will contribute to the development of an Empirical Valence Bond (EVB) model aimed at uncovering the molecular details of the mechanism of action of pAF in the reactions catalyzed by LmrR_pAF. By integrating theoretical and experimental approaches, her work will help elucidate how artificial amino acids expand the functional landscape of proteins and open new avenues for biocatalysis and synthetic biology.
We wish Nayanika a productive and inspiring stay in Groningen and look forward to the exciting results that will emerge from this collaboration with the Roelfes Lab.