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What are amino acids?
monomers of proteins, 20 different types each with a different R-group
Structure of amino acids
central carbon, amino group, carboxyl group, R group, hydrogen atom
How is a peptide bond formed?
A condensation reaction between two amino acids, molecule of water is removed (-OH for carbonyl group and -H from amino group)
What is a dipeptide?
2 amino acids joined by a peptide bond
What is a tripeptide?
3 amino acids bonded together
How is the peptide bond broken?
Hydrolysis- will release constituent amino acids
What is a polypeptide?
polymer of amino acids, always one need with a free amino group called the N-terminus and one end with a free carboxyl group called the C-terminus
What determines the function of proteins?
The primary structure shape- changing a single amino acid will change the shape and therefore function
what is the primary structure of proteins?
The sequence of amino acids in a polypeptide chain, which determines its overall shape and function
Bonded by peptide bonds
Formed by condensation reactions
what is the secondary structure of proteins?
the sequence of amino acids causes parts of a protein molecule to bend into alpha-helix shapes or fold into beta-pleated sheets
these structures are held in place by hydrogen bonds
where are the hydrogen bonds in the secondary structure?
form between the C=O group of carboxyl group of one amino acid and the H in the amine group of another amino acid
what is the tertiary structure of a protein?
the further folding of the secondary structure
to form a unique, 3D shape
held in place by ionic, hydrogen and disufide bonds
where do the ionic and disulfide bonds in the tertiary structure form?
between the R-groups of different amino acids
when do disulfide bonds form?
when there is a sulfur in the R-groups of both amino acids
what is the quaternary structure of a protein?
more than one polypeptide chain making up the protein
e.g. haemoglobin- made of 4 polypeptide chains
what does it mean if a protein is denatured?
the bonds which hold the tertiary and secondary structures in shape break, so the unique 3D shape is lost (especially ionic and hydrogen bonds break)
importance of primary structure
if one amino acid in sequence is different the ionic/hydrogen/disulfide bonds form in a different location
results in a different 3D shape
happens if a mutation occurs
Structure of a globular protein?
Compact, spherical molecules
Highly irregular sequence
Tertiary structure formed by folding of the polypeptide chain
What does the folding of the polypeptide chain in a globular protein do?
Brings hydrophobic amino acid residues inside and hydrophilic residues outside
Bonds in a globular protein?
Hydrogen bonds between polar groups
Ionic bonds between charged R-groups
Disulphide bridges
Hydrophobic interactions help maintain proteins shape
Are globular proteins soluble in water?
Yes as hydrophilic amino acids on outside
Functions of globular proteins
act as proteins to speed up biochemical reactions
Transport proteins
Hormones
Form part of immune system
Store molecules/ions
Examples of globular proteins
haemoglobin
Myoglobin
Insulin
Amylase
Antibodies
Structure of fibrous proteins
long, narrow, thread-like shape
Made of parallel polypeptide chains that form strong fibres/sheets
Mostly secondary structure with little tertiary folding
Regular sequence
What bonds are in fibrous proteins?
hydrogen bonds stabilise their repetitive structures
Cross linking (covalent bonds) like disulphide bridges provide extra strength and stabillity
Hydrophobic interactions contribute to strength
Are fibrous proteins soluble?
No- insoluble as hydrophobic amino acids are exposed and structure is rigid
Functions of fibrous proteins
provide structural support and strength to cells and tissues
Form key components of connective tissues, skin, hair, nails and tendons
Maintain shape and integrity of cells and organisms
Examples of fibrous proteins
collagen- found in connective tissue tendons and bones as has high tensile strength
Keratin
Elastin