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Proteins are the ‘doers’ of the cell. They are huge in number and variety and diverse in structure and function, serving as both the structural building blocks and the functional machinery of the cell. Just about every process in every cell requires specific proteins.

Let us begin by listing some of the basic cellular processes and the role that proteins play.

  • Chemical catalysis Enzymes, which are responsible for catalysing biological reactions, are the largest functional group of proteins. Whilst there are thousands of different enzymes, all catalysing different reactions, they do have some features in common and can often be identified as members of a particular family of enzymes.
  • Mechanical support Typically, support is provided by proteins, e.g. the cytoskeletal proteins inside the cell and the extracellular matrix proteins outside the cell.
  • Communication The signals within and between cells (e.g. cytokines) and the apparatus for recognising and interpreting or reacting to signals (receptors and transducers) are mainly proteins.
  • Adhesion Cell surface proteins mediate contact between cells and between a cell and the extracellular matrix (which is also made up of proteins).
  • Movement Proteins generate movement in a cell (motor proteins).
  • Defence Antibodies (immunoglobulins) are proteins that recognise specific targets (usually proteins themselves). This facility is critical for an immune response.
  • Transport Proteins are key molecules in the transport of substances both within a cell and to and from the cell.
  • Storage A number of proteins serve to store small molecules or ions; for example, ferritin binds iron and stores it in the liver.

You will come across many examples in this course of proteins performing the functions outlined above, and the molecular basis for various cellular processes will be examined in some detail. The basic principles of protein structure and function, which are reviewed in this course, are crucial to understanding how proteins perform their various roles.

The huge diversity in the functions of proteins is reflected in the specialisation of these molecules. As you will see in this course, every protein optimally performs a particular job and the key to how it does so is its structure. The refinement of protein structure and optimisation of protein function are driven by evolutionary pressures. Mutations at the DNA level that result in a change in protein structure and function will persist if they enhance survival or are not detrimental to the organism.

Proteins come in as many different shapes and sizes (Figure 1) as they have functions. A broad distinction is made between globular proteins and fibrous proteins. Globular proteins are a particularly diverse group that includes enzymes, receptors and transport proteins, and are characterised by a roughly spherical compact shape. Fibrous proteins are elongated and rod-like (e.g. collagen, represented in (Figure 1) and often have a structural role. Most of the proteins discussed in this course are globular proteins, which reflects both their number and the fact that they lend themselves to structural analysis by X-ray diffraction and NMR.

Figure 1 A few of the many different proteins represented in a highly schematic form and according to their relative sizes.

In this course, we will consider aspects of the structure of proteins and illustrate how, through their interactions with other cellular components, they can function as dynamic molecular machines. We will begin by exploring the three-dimensional nature of proteins, reviewing some of their biochemistry and the biophysical rules that determine their structure and studying key structural elements that are common to many proteins. You will encounter these activities as you progress through the course. The relationship between protein structure and function is explored using as examples a variety of different proteins, including enzymes, signalling proteins and transport proteins. All proteins bind other substances, often other proteins or organic molecules or inorganic ions. These interactions are integral to a protein’s function and their specificity and affinity are critically determined by the protein’s structure. This aspect is discussed at some length. The course finishes with a consideration of some of the techniques employed in studying protein–protein interactions.

Course Curriculum

1. The three-dimensional nature of proteins
The peptide bond and primary structure of proteins 01:30:00
Protein secondary structure 01:30:00
Protein tertiary structure 01:30:00
Quaternary structure 01:30:00
Fibrous proteins 01:30:00
2. Assembling a functioning protein
Assembling a functioning protein – Introduction 01:30:00
Chaperones help polypeptides to fold 01:30:00
Some proteins require small-molecule cofactors 01:30:00
The covalent modification of proteins 01:30:00
3. Protein domains
Protein domains – Overview 01:30:00
Structural domains 01:30:00
Binding domains in intracellular signalling proteins 01:30:00
The functional domains of Src 01:30:00
4. Protein families and structural evolution
Introduction – Protein families 01:30:00
Conserved protein domains 01:30:00
5. Dynamic proteins
All proteins bind other molecules 01:30:00
Regulating protein conformation and activity 01:30:00
Protein–protein interactions 01:30:00
6. Catalytic proteins
Catalytic proteins – Introduction 01:30:00
Catalytic mechanisms 01:30:00
Lysozyme 01:30:00
Carboxypeptidase A 01:30:00
Multienzyme complexes 01:30:00
7. Studying protein function
Site-directed mutagenesis 01:30:00
Studying protein–protein interactions 01:30:00
Library-based methods for demonstrating an interaction between proteins 01:30:00
Proteomics 01:30:00
Acknowledgements – Proteins 00:10:00
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