Biological Molecules 2

Proteins

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Learning outcomes
Describe the basic structure of an amino acid

and the formation of polypeptides and proteins (as amino acid monomers linked by peptide bonds in condensation reactions) Explain the significance of a proteins primary structure in determining its three-dimensional structure and properties (globular and fibrous proteins and types of bonds involved in three dimensional structure).
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Proteins - Functions
Wide range of Antibodies
Enzymes Many hormones

Various proteins make up muscles, ligaments, tendons, Hair Important components of cell membranes
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Building blocks: Amino acids

All proteins composed of Amino acids
20 different amino acids Plants can make all 20 amino acids

Animals can only make some, the rest

obtained in their diet (essential amino acids)

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Amino Acids R groups can be any of 20

different forms giving 20 naturally occurring amino acids

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Primary structure
Two amino acids join together in a

condensation reaction to form a dipeptide This process is repeated to form a polypeptide chain A protein is made up of one or more polypeptide chain The sequence of amino acids is known as the primary structure
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Secondary structure -helix

A chain of amino acids may twist to form

an -helix Within the helix, hydrogen bonds form between C=O of the carboxylic acid and NH2 of the amine group

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Secondary Structure -pleated sheet

Several chains may link together, with

hydrogen bonds holding the parallel chains in an arrangement known as pleated sheet

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Secondary structure

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Tertiary structure
Polypeptide chains often bend and fold

to produce three-dimensional shape. Chemical bonds and hydrophobic interactions between R group maintain this final tertiary structure of the proteins

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Tertiary structure
An R group is polar when the sharing of

electrons within it is not quite even Polar R groups attract other polar molecules and are therefore hydrophilic (water attracting) The non-polar groups are hydrophobic (water repelling) Non-polar hydrophobic R groups are arranged to face inside the proteins excluding water from the centre of the molecule
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Tertiary structure

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Quaternary structure
A protein may be made of several

polypeptide chains held together e.g. haemoglobin, insulin Only proteins with several polypeptide chains have quaternary structure

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Haemoglobin
Haemoglobin consists of four

polypeptide subunits two are called chains, the other two are called - chains Each unit is held in place by a number of bonds and interactions. These interactions give the molecule a specific shape. This shape is important for the molecule to carry out its function.
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Haemoglobin
A specialised part of each polypeptide

called a haem group contains an iron(Fe2+) ion. Haem group gives haemoglobin its colour Each haem group binds with one oxygen molecule Therefore one haemoglobin molecule contains four oxygen molecules
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Globular proteins
Folded into a compact spherical shape
These proteins are soluble due to the

hydrophilic side chains that project from the outside of the molecule. This make them important in metabolic reactions. Enzymes are globular proteins

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Globular Proteins
Enzymes three dimensional shape is crucial

to their ability to form enzyme substrate complexes and catalyse reactions in cells. Three dimensional shape is critical in their role of binding to substances. e.g proteins in membranes Antibodies are also globular proteins and rely on shape to bind to microorganisms
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Fibrous proteins
Do not fold in to ball shape but remain as

long chains Several chains can be cross-linked for additional strength. These insoluble proteins are important structural molecules.

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Fibrous Proteins
Keratin in Hair and Skin.
Collagen in skin. Tendons

Bones
Cartilage Blood vessel walls

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Fibrous Protein:Collagen

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Collagen

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Denaturation
If proteins are heated or the pH is changed

they can loose their shape and unfold. Such proteins are said to be denatured. In a cell denatured proteins are broken up and the amino acids reused unless they can be refolded. Protein aggregates are toxic and accumulations can causes diseases e.g. Altzheimers disease, Scrapie
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Enzymes
Many proteins catalyse

chemical reactions. These proteins are known as enzymes. All enzymes have a definite shape and have a part known as the active site where the substrate(s) bind.
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