| Grant number: | 14/19439-5 |
| Support Opportunities: | Regular Research Grants |
| Start date: | November 01, 2014 |
| End date: | October 31, 2016 |
| Field of knowledge: | Biological Sciences - Biochemistry - Enzymology |
| Principal Investigator: | Sandro Roberto Marana |
| Grantee: | Sandro Roberto Marana |
| Host Institution: | Instituto de Química (IQ). Universidade de São Paulo (USP). São Paulo , SP, Brazil |
| City of the host institution: | São Paulo |
Abstract
The functional properties of enzymes may be traced to groups of aminoacid residues forming chains based on covalent and non-covalent contacts. Based on that, this project aims to map these "chains of residues" on protein structures and characterize their role on the determination of functional properties as catalytic activity, substrate specificity and thermal stability. Beta-glucosidases from family GH1 and the lisozyme MdL1 from family GH23 will be used as experimental models in this project. The mapping of the "chains of residues" potentially related to functional properties will rely on the representation of the protein structures as networks (graphs). Additionally, the evaluation of the functional properties will be based on quantitative parameters as kinetic constants for the hydrolysis of different substrates (kcat and Km), rate constants for thermal denaturation, transition temperature for protein desnaturation (Tm) and dynamics evaluated in NMR experiments. (AU)
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