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Protein structure
Fibrous proteins structural, e.g. collagen.
Globular proteins metabolic functions, e.g. haemoglobin.
So, what goes into a protein?
Proteins are polymer molecules.
The monomer molecules making up proteins are called amino acids.
There are 20 different naturally occurring amino acids.
There are over 100,000 combinations of amino acids forming known proteins.
Are all amino acids equal?
No, of the __________ naturally occurring amino acids 8 are known as essential amino acids. These
8 cannot be synthesised by the body and must be obtained from the diet.
The remaining 12 can be synthesised by the body.

Dipeptides
Condensation Reaction (makes water).
Peptide bond formed


Draw in the atoms
removed
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Proteins have 4 structural levels.
Proteins are big, complicated, 3-dimensional molecules.
The structure is described in four levels:
Primary
Secondary
Tertiary
Quaternary

Primary structure
Primary structure is the sequence of amino acids
Amino acids held together by peptide bonds
They are formed by loss of water so is called a condensation reaction.
Secondary Structure

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Tertiary structure

Complex 3D shape formed when helix or sheet twists and folds around itself
Held together by many different types of bonds

Disulphide bonds
Form between R-groups containing sulphur atoms e.g. cysteine and methionine.

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Ionic bonds
Form between R groups with charges e.g positive and negative charges.

Tertiary Structure helix
3D structure is formed by further bonds, depending on the function
Disulphide bonds strong and not easily broken down
Ionic bonds easily broken down by changes in pH (carboxyl/amino groups)
Hydrogen bonds numerous but very easily broken down
Quaternary structure
Some proteins are made up of several polypeptide chains held together by bonds.
The quaternary structure is how these chains are put together.
The best known example is haemoglobin, which is made of four polypeptide chains bonded
together. For proteins such as haemoglobin, the quaternary structure determines the final
3D structure.
Almost all working proteins are actually composed of more than one polypeptide chain

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Protein bonds
The four structural levels in proteins are held together by different bonds:
Peptide bonds (_______________)
Hydrogen bonds (_________________ and __________________)
Ionic bonds (______________)
Disulphide bonds (_________________)
Quaternary structure depends on the tertiary structure of the individual polypeptides, and so is
influenced by all these bond types.
What do proteins do?
Proteins perform a wide range of biological functions:
As enzymes they catalyse reactions.
Carrier proteins transport molecules across membranes.
Antibodies defend against disease.
Structural proteins support cells and tissues.
Hormones transmit information.
Transport proteins such as haemoglobin carry oxygen.
Contractile proteins enable muscles to contract.
Two main types
Fibrous proteins structural, e.g. collagen. These are tough and rope-shaped. They tend to
be found in connective tissues such as tendons.
Globular proteins metabolic functions. These are round, compact and easily soluble so
they can be transported in fluids. Examples are haemoglobin and enzymes.
It is their structure that allows them to carry out their functions.
i.e. the 3D structure is v.v.v important in carrying out its function
Makes proteins distinctive interacting with other molecules
Haemoglobin
Haemoglobin is a globular protein.
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Its structure is curled up so that hydrophilic side chains face outwards and hydrophobic side chains
face inwards.
This makes haemoglobin soluble and therefore good for transport in the blood.
Collagen
Collagen it made of three polypeptide chains, tightly coiled in a strong triple helix.
The chains are interlinked by strong covalent bonds.
Minerals can bind to the triple helix to increase its strength.
Summary
The primary structure of a protein is the sequence of amino acids, joined by peptide bonds
The secondary protein structure occurs when the sequence of amino acids are linked by
hydrogen bonds in an alpha helix or beta pleated sheet.
The tertiary structure describes the folding of a polypeptide chain that result from the
molecular interactions among the R groups of the different amino acids( H, disulphide, ionic
bonds)
The arrangement of two or more polypeptide chains in a protein make up its quaternary
structure
The importance
of proteins to
living organisms
Structure
Receptor
proteins and
cell
membranes
Protein
synthesis
Enzymes
Antibodies

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