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• W2808790845 abstract "The cohesin-dockerin receptor-ligand family is the key element in the formation of multi-enzyme lignocellulose-digesting extracellular complexes called cellulosomes. Changes in a receptor protein upon binding of a ligand - commonly referred to as allostery - are not just essential for signalling, but may also alter the overall mechanical stability of a protein receptor. Here, we measured the change in mechanical stability of a library of cohesin receptor domains upon binding of their dockerin ligands in a multiplexed atomic force microscopy-based single-molecule force spectroscopy experiment. A parallelized, cell-free protein expression and immobilization protocol enables rapid mechanical phenotyping of an entire library of constructs with a single cantilever and thus ensures high throughput and precision. Our results show that dockerin binding increases the mechanical stability of every probed cohesin independently of its original folding strength. Furthermore, our results indicate that certain cohesins undergo a transition from a multitude of different folds or unfolding pathways to a single stable fold upon binding their ligand." @default.
• W2808790845 created "2018-06-29" @default.
• W2808790845 creator A5020710861 @default.
• W2808790845 creator A5082022539 @default.
• W2808790845 date "2018-06-25" @default.
• W2808790845 modified "2023-09-27" @default.
• W2808790845 title "Ligand Binding Stabilizes Cellulosomal Cohesins as Revealed by AFM-based Single-Molecule Force Spectroscopy" @default.
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• W2808790845 doi "https://doi.org/10.1038/s41598-018-27085-x" @default.
• W2808790845 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6018229" @default.
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• W2808790845 hasPublicationYear "2018" @default.
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