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Fundamentals of Protein Chemistry
A one day short course on amino acids, protein structure, changes to protein structure and a brief review of analytical techniques used to characterize and analysis proteins

This one day short course focuses on the basics of protein structure. It includes a discussion of the twenty amino acids and their roles in protein structure and discusses primary, secondary, tertiary and quaternary protein structure. Protein modifications such as chemical degradation (deamidation, oxidation), aggregation and denaturation, and post-translational modifications such as glycosylation are also explained. The class concludes with a brief overview of key technologies involved in the analysis and characterization of proteins.

Course Outline

Essentials in Protein Structure

n Amino acids. Structure and character.

n The peptide bond

n The nature of the side-chains of the common amino acids.

n The interactions which form and stabilize polypeptide

n Secondary structure. The alpha-helix and beta-sheets

n Protein tertiary structure and its role in biological activity

n How primary and secondary structure lead to teritiary structure.

n Protein quaternary structure

Protein Degradations and Post-translational Modifications

n Glycosylation. The addition of oligosaccharides to the polypeptide.

n Deamidation and protein stability.

n Oxidation. The effect of oxygen and catalysis.

n Denaturation. Causes of the lose of protein tertiary structure.

n Aggregation. Unintended complex protein structures.

Overview of the Techniques for the Separation and Analysis of Proteins

n Chromatography: Reversed-phase HPLC, Ion Exchange, Size Exclusion

n Electrophoresis: Gel and Capillary

n Mass Spectrometry

n Biological assays

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What the attendees will learn!

n What are amino acids and what are the properties of the common amino acids.

n How do amino acids combine to form polypeptides and what is primary structure.

n What forces impart structure to polypetides and what are the principal secondary structural elements.

n What is tertiary structure and what is its significance.

n What is quaternary structure and what is its significance.

n What is glycosylation and how does it affect protein biological activity.

n What is deamidation, oxidation, denaturation and aggregation. What causes protein degradation and what effect does protein degradation have on protein activity.

n What techniques are most commonly used to analyze and characterize protein therapeutics and what are the basic principles behind the techniques.

Who will benefit from this course?

n Technical individuals who are involved in the laboratory analysis or characterization of protein therapeutics but have little knowledge of protein chemistry.

n Individuals involved in production, formulation or packaging of protein therapeutics who would benefit from greater understanding of the products they work with.