Section: Rotations

Francesca Massi, Ph.D.

Academic Role: Assistant Professor

Faculty Appointment(s) In:
   Biochemistry and Molecular Pharmacology

Rotation Projects

Rotation projects are available to understand:

1. The effect of enzyme loop motions on catalysis.
Ligand binding promotes a structural transition in ODCase between an open and a closed state. What are the kinetic and thermodynamic properties of this transition? We will perform NMR relaxation experiments to monitor enzyme motions on different time scales. These results will provide direct insight into the opening and closing transitions of the enzyme and will correlate these transitions with the microscopic rate of catalytic turnover.

2. The relationship between flexibility and aggregation propensity in b₂-microglobulin. The presence of conformational flexibility indicates the transition between two or more states, one of which might be an intermediate that drives the monomeric b₂m to associate into insoluble aggregates. In order to fully explore the connection between dynamics and aggregation propensity, we will study the structure and dynamics of the wild type b₂m and different mutants that show different aggregation properties relative to the wild type protein.

Office: LRB 925
Phone: 508-856-4501
E-mail: Francesca.Massi@umassmed.edu
Keywords: Protein Folding, Biophysics, Structural Biology, Biochemistry

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