Real-time tracking of single-molecule collagenase on native collagen and partially structured collagen-mimic substrates

Autor:	Jasmin Farmakes, James Froberg, Tayebeh Anajafi, Sanku Mallik, D. K. Srivastava, Abbas Sedigh, Woo-Sik Choi, Zhongyu Yang, Yongki Choi
Rok vydání:	2018
Předmět:	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
Zdroj:	Chemical Communications. 54:10248-10251
ISSN:	1364-548X 1359-7345
DOI:	10.1039/c8cc04601h
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::277acf621e8837735db2161266dfdd18 https://doi.org/10.1039/c8cc04601h Zobrazit plný text záznamu