Transcript Proteins

PROTEINS
• Have a wide range of functions;
haemoglobin, antibodies & enzymes
• Amino acids are the monomers
• Twenty naturally occurring amino acids
• The order of the AA and the way they
are folded dictates the function
General Amino Acid Structure
Variable
R group
NH2
COOH
Central (α) carbon
Forming a dipepetide
•AA 1 and AA2 line up
•Amine next to carboxyl
group
•Amine Grp ‘donates’ OH
•Carb. Grp ‘donates’ H
•Water is eliminated
•A dipeptide is formed
Forming a polypepetide
•1000s of AAs link up
•Ribosomes convert AA to
polypeptides
•A string of AA like this
is PRIMARY STRUCTURE
Secondary Protein Structure
Two types exist;
alpha (α) helix
beta (β)pleated sheets
Alpha (α) helix
• AA interact with each other
• The H on the NH grp is attracted to
the O on the CO grp
• The H is slightly positive and the O is
slightly negative
• A H bond forms between these two
atoms
Hydrogen bonds are
numerous……..
……..individually
weak!
The H bonds that keep Alpha helices
together are vulnerable to fluctuations in
pH & temperature
Beta (β) pleated sheets
Hydrogen bonds hold adjacent primary chains
together
To go above secondary structure,
proteins need more bond types;
Disulphide bonds
Adjacent cysteine AA
Weak bond
Broken by reducing agents
Ionic bonds
Forms between ionised amine
& carboxylic grps
Broken by pH extreme
Hydrophobic
Interactions
Btwn non polar
R-grps
TERTIARY PROTEIN STRUCTURE
• Classic example – MYOGLOBIN
• Folded into a precise 3D shape
• H bonds form between tryptophan, arginine
& asparagine.
• Dulsulphide bonds with cysteine
• Ionic bonds & hdrophobic interactions also
exist
Myoglobin – a tertiary
Level protein
QUATERNARY
PROTEIN STRUCTURE
• Classic examples – HAEMOGLOBIN
COLLAGEN
• Globular proteins are involved in chemical
reactions & are soluble molecules;
haemoglobin
• Fibrous proteins have a structural role in
biology; collagen
HAEMOGLOBIN
• made of 4 polypeptide chains
• two alpha chains
• two beta chains
• Hydrophobic R grps point into the molecule
• Hydrophilic R grps point out of the molecule
• This makes haemoglobin highly soluble
HAEMOGLOBIN
• each of the 4 chains has a haem group
• the haem group is not made of AA, but is an
integral part of the protein – prosthetic grp.
• Each haem group contains an ion of iron
(Fe2+)
• Each haem binds with one molecule of
oxygen (O2)
• So each haemoglobin can carry O8
Haemoglobin – a quaternary
Level protein