Official Project Description
Ribulose-1,5-bisphosphate carboxylase/oxygenase activase (RCA) is an essential enzyme that helps maintain the activity of Rubisco, the protein responsible for carbon fixation in photosynthesis.
RCA forms a range of oligomeric assemblies (including dimers, trimers, and hexamers) that are dynamic and sensitive to temperature, and their stability is closely linked to how well plants can function under heat stress.
In this study, we will use MD simulations to examine RCA across different oligomeric states and temperatures.
By comparing wild-type and mutant forms, we aim to determine how temperature influences structural stability and subunit interactions within each assembly.
These simulations will help identify key features that stabilize RCA and reveal how mutations alter its behavior.
The results will provide insight into temperature-dependent regulation of RCA and support efforts to design more heat-tolerant variants for improved photosynthesis.