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Investigating Receptor-ligand Systems of the Cellulosome with AFM-based Single-molecule Force Spectroscopy

Article DOI: 10.3791/50950-v • 11:34 min • December 20th, 2013
December 20th, 2013 •
*1, *1, 1, 1
1Lehrstuhl für Angewandte Physik and Center for Nanoscience, Ludwig-Maximilians-Universität
* These authors contributed equally

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Summary
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Cellulosomes are multienzyme complexes designed for digesting cellulose. AFM-based SMFS was used to study the mechanical properties and folding configuration of cellulosome-associated protein assemblies. We present a complete workflow for protein immobilization, data acquisition, and data analysis to study the interactions of individual receptor-ligand complexes involved in cellulosome assembly.

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Receptor-ligand Systems Cellulosome AFM-based Single-molecule Force Spectroscopy Anaerobic Bacteria Fungi Lignocellulosic Substrates Noncatalytic Scaffold Protein Interacting Cohesin And Dockerin Modules Dissociation Constants Picomolar Range Nanomolar Range Single-molecule Force Spectroscopy (SMFS) Atomic Force Microscope Biomolecules High-affinity Receptor-ligand Interactions Optical Tweezers Protein Topology Enzyme-dockerin Fusion Proteins Carbohydrate Binding Module-cohesin Fusion Proteins Free Thiol Group Engineered Cysteine Residue Site-specific Surface Immobilization Protocol
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