ENZYMOLOGY
cod. 04241

Academic year 2008/09
1° year of course - First semester
Professor
Academic discipline
Biochimica (BIO/10)
Field
Discipline biologiche e biologiche applicate
Type of training activity
Characterising
24 hours
of face-to-face activities
3 credits
hub:
course unit
in - - -

Learning objectives

To gain a deeper understanding of Enzymology students will be expected to read and discuss with the teacher some original papers of general interest. 

Prerequisites

- - -

Course unit content

<br />The three-dimensional structure of enzymes. Chemical Catalysis. The basic equations of enzyme kinetics. Measurement and magnitude of individual rate constants. The pH dependence of enzyme catalysis. Practical methods for kinetics and equilibria. Detection of intermediates by kinetic methods. Stereochemistry of enzymatic reactions. Ligand binding and allosteric regulation. Forces between molecules and binding energies. Enzyme-substrate complementarity and the use of binding energy in catalysis. 

Full programme

- - -

Bibliography

A. Fersht. Structure and Mechanism in Protein Science: a Guide to Enzyme Catalysis and Protein Folding. Publisher: W.H.Freeman & Co Ltd, UK 1999 3REV ED

Teaching methods

<br />To pass the exam, students will describe and critically discuss two or more topics included in the program, possibly with reference to original papers. 

Assessment methods and criteria

- - -

Other information

- - -