Date of Graduation
8-2022
Document Type
Thesis
Degree Name
Bachelor of Science
Degree Level
Undergraduate
Department
Chemistry & Biochemistry
Advisor/Mentor
Sakon, Josh
Committee Member/Reader
Erickson, Kirstin
Committee Member/Second Reader
Levine, Bill
Committee Member/Third Reader
Millett, Frank
Abstract
Known to cause gas gangrene, Hathewaya histolytica secretes two sister collagenases, collagenase G (Col G) and collagenase H (Col H), to degrade the triple helical structure of collagen to further infection in a host. Individual domains of Col H have been crystalized in previous studies, but methods in x-ray crystallization of full-length Col H have been unsuccessful. Using Small Angle X-Ray Scattering (SAXS) data, atomistic modeling was used to generate multiple conformations of Col H while accounting for flexibility between domains. Full-length Col H was found to adopt a two-state conformational model exhibiting a majority compact and a minority elongated form regardless of calcium concentration. This suggests Col H may become more flexible in lower calcium concentrations but does not elongate as previously suspected. Determination of full-length Col H could significantly impact drug delivery design and therapeutic agents concerning procedures such as skin debridement and pancreatic islet extraction.
Keywords
SAXS; Collagenase H; ColH; Col H; Full-length; Structure
Citation
Carson, J. (2022). Determining the Full-Length Structure of Collagenase H using Small-Angle X-ray Scattering. Chemistry & Biochemistry Undergraduate Honors Theses Retrieved from https://scholarworks.uark.edu/chbcuht/30
