Authors:

Richard Lawrence

Date Created:

Not specified

Course Title:

Professor:

Not specified

About Paper:

Rubisco has been found to spontaneously polymerize into higher-ordered structures such as chains and lattices within ?-carboxysomes. Whereas previously, best methods involved visually qualifying which rubiscos participate in these polymers, the purpose of this study was to consistently quantify any participating rubisco molecule. This was carried out by using matlab scripts to perform particle picking and biophysical analysis on reconstructed electron tomograms to find which rubiscos are participating in intermolecular interactions. Custom programs were written to test the accuracy of the results and to visualize their various properties. A particularly exciting breakthrough was when a histogram of the distances between chains confirmed our theory that the chain lattices follow a six-fold symmetry. Another result was that the matlab script, responsible for identifying interacting pairs, produced a graph of the binding affinity of rubisco which was validated by previous results. And a final result is that the rubiscos participating in these higher-ordered structures can now be visualized in the tomograms themselves, making quantification even more effective. This research explores the interactions and polymerization of proteins through liquid-liquid phase separation. This type of biological and biophysical process is a quickly growing field of study which has deep implications in how biological structures can spontaneously form. Current methods involve studying these polymerizations in vitro, but soon it will translate to in situ studies, and it is essential to be able to quantitatively identify polymers within the more noisy environments that a proper in situ study requires. Keywords: Carboxysomes; Rubisco; Polymerization; Computational Biophysics; cryoET

Source:

Purdue University / 2024

Topics:

No topics listed

Co-authors:

Richard Lawrence