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Naman B. Shah

Department of Biochemistry and Molecular Biology

SUNY Upstate Medical University

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F1-ATPase of Escherichia coli: the ε- inhibited state forms after ATP hydrolysis, is distinct from the ADP-inhibited state, and responds dynamically to catalytic site ligands.

The Journal of biological chemistry Mar, 2013 | Pubmed ID: 23400782

INSTITUTIONS

SUNY Upstate Medical University

JOVE ARTICLES

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects

Naman B. Shah¹,

Thomas M. Duncan¹

¹Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University

Chemistry

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Naman B. Shah

.css-o250i3{font-size:18px;font-family:Open Sans,sans-serif;line-height:21.6px;}Department of Biochemistry and Molecular Biology

SUNY Upstate Medical University

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects

Department of Biochemistry and Molecular Biology