Tertiary Structure

 Usually, the polypeptide chain bends and folds extensively, forming a precise, compact
‘globular shape’
 This is the protein’s tertiary structure and it is maintained by the interaction of the four
types of bonds discussed below.
 With hydrophobic bonds being quantitatively the most important, as these occur when the
protein folds so as to shield hydrophobic side groups from the aqueous surroundings, at
the same time exposing hydrophilic side chains
Bonds used in protein structure
Ionic Bonds
 Acidic and basic R groups exist in an ionized (charged state) at certain pHs. Acidic R
groups are negatively charged and basic R groups are positively charged.
 They can therefore be attracted to each other, forming ionic bonds
 In an aqueous environment, this bond is much weaker than a covalent bond and can be
broken by a change in the pH of the medium.

Disulphide Bond
 The amino acid cysteine contains a sulphydryl group, -SH, in its R group
 If two molecules of cysteine line up alongside each other, neighbouring sulphydryl
groups can be oxidised and form a disulphide bond.
 These bonds can be formed between different chains of amino acids or between different
parts of the same chain.
 In the latter case, the dispulphide bonds make the molecule fold into a particular shape.
 These bonds are strong and not easily broken.

Hydrogen Bond
 When hydrogen is part of an OH or NH group, it becomes slightly positively charged
(electropositive)
 This is because the electrons that are shared and which are negatively charged, are
attracted more towards the O or N atoms.
  The hydrogen may then be attracted towards a neighbouring electronegative oxygen or
nitrogen atom, such as the O of a C=O group or the N of an NH group.
 C=O groups and NH groups occur along the length of polypeptide chains, and they can
interact to produce regular shapes such as the alpha helix
 They hydrogen bond is weak but as its occurrence is frequent, the total effect, makes a
considerable contribution towards molecular stability, as in the structure of the alpha
helix

Hydrophobic interactions
 Some R groups are non polar and therefore hydrophobic.
 If a polypeptide chain contains a number of these groups and is in an aqueous
environment, the chain will tend to fold so that a maximum number of hydrophobic
groups come into close contact and exclude water.
 This is how many globular proteins fold up
 The hydrophobic groups tend to point inwards, towards the centre of the roughly
spherical molecule, while the hydrophilic groups face outwards into the aqueous
environment.

4. Quaternary Structure
 This structure is found in proteins containing more than one polypeptide chain and
simply means how the different polypeptide chains are arranged together.
 The separate chains are held together by the same bonds described above i.e. disulphide
bonds, ionic bonds, hydrogen bonds and hydrophobic and hydrophilic interactions.
 Haemoglobin shows such a structure.
 It consists of four separate polypeptide chains, namely two alpha chains and two beta
chains
 https://alevelbiology.co.uk/notes/hemoglobin/
 STRUCTURE OF THE PROTEIN COLLAGEN IN SOME DETAIL
 Collagen is a member of a family of naturally occurring proteins. It is one of the most
plentiful proteins present in mammals, and it is responsible for performing a variety of
important biological functions. It is most well known for the structural role it plays in the
body. Collagen is present in large quantities in connective tissue and provides tendons and
ligaments with tensile strength, and skin with elasticity.

 About one-quarter of all of the protein in your body is collagen but in spite of its critical
function in the body, collagen is a relatively simple protein.

 The collagen molecules themselves are made from 3 individual polypeptides of amino acids.
These chains are closely held together by hydrogen bonds to form a triple helix. Hydrogen
bonds form between these individual polypeptide chains, which are around 1000 amino acids
in length, which gives the structure strength. This is important given collagen’s role, as
structural protein.

 In animals, individual collagen triple helices, are known as tropocollagen. These triple
helices assemble in a complex, hierarchical manner that ultimately leads to the macroscopic
fibers and networks observed in tissue, bone, and basement membranes.

STRUCTURE DETAILS

 Each polypeptide chain is a helix shape and contains about 1000 amino acids with glycine,
proline and hydroxyproline being the most common. This fibrous, structural protein
comprises a right-handed bundle of three parallel, left-handed polyproline II-type helices.

 In the primary structure of collagen almost every third amino acid is glycine
1. This is the smallest amino acid with a R group that contains a single hydrogen atom
2. Glycine tends to be found on the inside of the polypeptide chains allowing the three
chains to be arranged closely together forming a triple helix structure (tropocollagen)
 This strength is increased by the fact that covalent bonds also form cross-links between R
groups of amino acids in interacting triple helices when they are arranged parallel to each other.
The cross-links hold the collagen molecules together to form fibrils
 The collagen molecules are positioned in the fibrils so that there are staggered ends (this
gives the striated effect seen in electron micrographs)

 When many fibrils are arranged together they form collagen fibres

LIPIDS

Triglycerides

Structure

Ester Bond
 Transcription and Translation

 Getting from DNA to protein requires two major stages

1. Transcription
2. Translation
 Transcription – is the synthesis of RNA using information in the DNA.
 DNA serves as the template for assembling a complementary strand of RNA
