Ultrastable Protein Complexes

By the employment and development of state-of-the-art computational tools, and in a collaborative effort with experimental labs, our group explores how proteins sense, generate, and activated by mechanical forces. 


Mechamisms of Force Resilience

Combining molecular dynamics simulations with bioinformatics tools and AI-based analysis methods, we are investigate how small differences in protein sequence can render different mechanical properties to these proteins.  



SARS-CoV-2 infections are initiated by attachment of the receptor-binding domain (RBD) on
the viral Spike protein to angiotensin-converting enzyme-2 (ACE2) on human host cells.  We  are combining experimental results with steered molecular dynamics simulations to investigate the mechanics of the RBD:ACE2 interaction. Our simulations can be used to describe how the virus have evolved to become more mechanically stable.


Force Propagation Analysis

Combining network-based correlation analysis with AFM directional pulling experiments, has allowed us to visualize stiff and soft paths through protein complexes along which force was transmitted.


Enzymatic Reactions

Combining hybrid QM/MM calculations with molecular biology experiments allows us to investigate the mechanisms 

NIH Center
Computational Biophysics Group

Leach Science Center
380 Duncan Dr. 
Room 3180 / 3182
Auburn, AL

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