Content, progress and pedagogy of the module

Learning objectives

Knowledge

Students who have passed the module should be able to

• account for the chemistry and thermodynamics behind protein structure, folding, stability and function, including the effect of protein modifications
• account for strength, specificity and cooperativity in ligand binding
• account for the principles and biophysical methods allowing isolation and purification of proteins
• outline principles and concepts in rational design, directed evolution, and semi-rational design of proteins

• account for screening techniques used for selection and/or screening of novel protein variants with improved properties

Skills

• select and apply biophysical methods for analysis of secondary, tertiary and quaternary structure of proteins
• apply theory on protein folding and stability to predict effect of mutations, insertions or deletions
• explain and select biophysical methods for analysis of ligand binding
• determine the binding strength from experimental data
• design purification strategies, allowing the isolation of pure preparations of proteins
• design recombinant proteins and processes for their purification
• develop strategies for obtaining mutants of protein with improved properties for industrial applications, using directed evolution technologies.
• apply theories on protein stability, ligand binding and protein engineering in the field of applied immunology to generate biologicals of therapeutic value.
• use online modelling tools to predict protein structure and ligand binding

Competences

• Read and understand advanced scientific articles in structural and analytical protein chemistry, protein engineering and directed evolution, with applications in industrial biotechnology and in applied immunology, with applications in medical biotechnology.

Type of instruction

• Lectures
• Theoretical exercises
• Student presentations

Extent and expected workload

150 hours

Exam

Exams