Nick Leioatts' Homepage

Research Interests

My research interests involve understanding the mechanics of the F-ATPase motor.  

The FOF1-ATPase is a complex nanomotor that synthesizes nearly 90% of the ATP made during cellular respiration. It consists of two coupled rotary motors: an integral membrane complex driven by proton flow across lipid bilayers (FO) and an enzymatic complex that converts ADP and inorganic phosphate to ATP (F1). The rotational portion of these motors acts as a camshaft, inducing conformational changes that lead to ATP synthesis in the F1 motor’s three functional catalytic sites. The F1 motor can perform ATP synthesis in the absence of FO, and it can also work in reverse, hydrolyzing ATP to pump protons against an established gradient. Over the last 30 years many important aspects of this motor’s function have been elucidated by careful biochemical work and further understood by clever biophysical experimentsHowever, there is still not a complete, quantitative description of the whole thermodynamic cycle—one that fully describes the interactions between all three separate catalytic sites and accounts for the need to exchange ATP (found abundantly) for the relatively sparse ADP.

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Publications

Leioatts, N., Romo, T. D., Danial, S. A., and Grossfield, A.
Retinal Conformation Changes Rhodopsin’s Dynamic Ensemble
Romo, T. D., Leioatts, N., and Grossfield, A.
Lightweight Object Oriented Structure Analysis: Tools for building tools to analyze molecular dynamics simulations
Leioatts, N., Suresh, P., Romo, T. D., and Grossfield, A.
Structure-based simulations reveal concerted dynamics of GPCR activation
Mnpotra, J.S., Qiao, Z., Cai, J., Lynch, D. L., Grossfield, A., Leioatts, N., Hurst, D. P., Pitman, M. C., Song, Z.-H., Reggio, P.H.
Structural basis of G protein-coupled receptor-Gi protein interaction: formation of the cannabinoid CB2 Receptor/Gi Protein Complex
Leioatts, N., Mertz, B., Martinez-Mayorga, K., Romo, T. D., Pitman, M. C., Feller, S. E., Grossfield, A., Brown, M. F.
Retinal ligand mobility explains internal hydration and reconciles active rhodopsin structures
Leioatts, N., and Grossfield, A.
Molecular dynamics simulations of membranes and membrane proteins
Seckler, J. M., Leioatts, N., Miao, H., and Grossfield, A.
The interplay of structure and dynamics in the function of HIV-1 reverse transcriptase
Leioatts, N., Romo, T. D., and Grossfield, A.
Elastic network models are robust to variations in formalism

My old work on Rhodopsin can be found here.

 
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