1. Real-time tracking of single-molecule collagenase on native collagen and partially structured collagen-mimic substrates
- Author
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Jasmin Farmakes, James Froberg, Tayebeh Anajafi, Sanku Mallik, D. K. Srivastava, Abbas Sedigh, Woo-Sik Choi, Zhongyu Yang, and Yongki Choi
- Subjects
0301 basic medicine ,Protein Conformation ,Kinetics ,Matrix (biology) ,Crystallography, X-Ray ,Microscopy, Atomic Force ,Article ,Catalysis ,Substrate Specificity ,03 medical and health sciences ,Protein structure ,Materials Chemistry ,medicine ,Molecule ,chemistry.chemical_classification ,Chemistry ,Molecular Mimicry ,Metals and Alloys ,Substrate (chemistry) ,General Chemistry ,Surfaces, Coatings and Films ,Electronic, Optical and Magnetic Materials ,030104 developmental biology ,Enzyme ,Ceramics and Composites ,Collagenase ,Biophysics ,Collagen ,Matrix Metalloproteinase 1 ,medicine.drug - Abstract
The dynamic interactions of an individual matrix metalloproteinase-1 were imaged and monitored in the presence of either triple-helical or non-triple-helical, partially-structured collagen-mimic substrates. The enzyme exhibited ten-fold increased catalytic turnover rates with the structurally modified substrate by skipping the triple-helix unwinding step during the catalytic pathway.
- Published
- 2018
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