Biochemistry 2 - SIB2004

Assessment 1: Practice exam/test

In class problem solving tutorials similar to examination questions.

Practice exam/test

Assessment 1: Exam

Exam

Assessment 2: Written Assignment

Written assignment

This module considers protein structure in relation to function, in particular enzyme action and membrane mediated metabolic processes.
The various types of post-translational modifications of proteins are discussed in detail, followed by an account of protein folding. Protein mis-folding, aggregation and intrinsic disorder are discussed using prion proteins, amyloid and FnBPA as examples.  Various globular and fibrous proteins illustrate regulatory strategies.  Channels, pumps and cytoskeletal components illustrate higher levels of organisation of proteins. 
The techniques of X-ray crystallography and Cryo-EM for protein structure determination are introduced. Advantages and limitations are discussed.
Lectures discuss various techniques for analyzing protein structure, folding and protein-protein interactions (isothermal titration calorimetry, near and far UV circular dichroism)
The structure and function of mitochondria and chloroplasts is covered, including respiration and photosynthesis pathways, focusing on electron transport chains.
Mechanisms of enzyme catalysis are discussed with numerous examples (acid-base, covalent, nucleophilic, metal ion etc.).
In lectures, practicals and problem based tutorials the skills required for determining kinetic and inhibition constants (kcat, catalytic efficiency, Ki) will be developed.
Practicals also allow the student to isolate a pure protein from egg white, assess product quality and consider the commercial value of this purified material.

School of Applied Sciences

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Biology

SIB2004 - Biochemistry 2

Biochemistry 2

be able to analyse and determine kinetic constants such as Km Vmax and Kcat.

understand the wide variety of post-translational modifications involved in protein function and/or stability.

be able to describe the factors relevant to protein folding and give examples of different models of protein folding.

be able to list the structures of proteins in terms of levels of structure building on one another to form a hierarchy.

have knowledge of interactions in the functioning of macromolecules.

be able to describe some of the techniques used to determine and study the structure of macromolecules. Know their requirements and limitations.

be able to purify a protein from a mixture and perform basic analysis (concentration, yield, SDS-PAGE).

be able to describe the complex machinery of photosynthesis the electron transport chain and ATP synthesis.

be able to outline the role of conformation and weak.

be able to use computational methods to predict the extinction coefficient at 280nm, molecular weight and isoelectric point from an amino acid sequence and understand how to apply this knowledge.

be able to relate structure to function wherever possible.