Proteins Flashcards
draw a basic structure of an amino acid and label the different parts
-amino group
-carboxyl group
-variable group
draw the reaction between 2 amino acids
reaction? products? bond?
-condensation reaction
-water and dipeptide
-peptide bond
what is the primary structure of protein?
-the order/sequence of amino acids n the polypeptide chain joined by peptide bonds
-determines shape and function of protein
-around 20 different amino acids making different combinations
what is the secondary structure of protein?
-coiling or folding of amino acid chain due to hydrogen bonds
-alpha helix or beta pleated sheets
-hydrogen bonds between c=o carboxyl group of one and H of amino group of the other
what is the tertiary structure of protein?
-precise/functional shape, further folding of protein
-globular or fibrous
bonds:
-ionic - R group charged
-disulphide bridges if sulfur in R group present
-hydrogen bonds
hydrophilic or hydrophobic
what is the order of bonds/interactions in tertiary structure according to strength?
disulphide-ionic-hydrogen-hydrophilic/phobic
what is the quaternary structure of protein?
-a protein made up of more than one polypeptide chains
-e.g haemoglobin or collagen
-what is a prosthetic group?
-give an example
-a non protein associated with a protein
-e.g haem group in haemoglobin
compare fibrous and globular protein
Fibrous:
-regular repetitive sequence
-usually insoluble due to hydrophobic groups
-very strong
-cross linking of polypeptides chains by hydrogen bonds = fibrous structure
-collagen, elastin, keratin
Globular:
-tend to roll up into almost sphere
-soluble as hydrophilic groups outside on the surface
-much weaker secondary and tertiary bonds = denature
-polypeptide chains are folded in to form their specific shapes
-enzymes, hormones, insulin, haemoglobin
describe collagen a fibrous protein
and its function
-fibrous tight triple helix made of three polypeptide chains
-insoluble
-glycine - 1/3 of amino acid= polypeptides can wind tightly round as glycine is the smallest R group.
-no prosthetic group
-mainly left handed helix, triple helical
Functions:
-artery walls prevented from bursting
-tendons and ligaments connecting muscles to bones stretch without snapping
-bones- collagen network hardened
-cartilage and connective tissue
describe haemoglobin a globular protein
and its functions
-four polypeptide chains
-globular/round
-soluble
-made of many amino acids
-mainly alpha helix
-carry oxygen around the body
-haem prosthetic group
what is the test for protein?
- add biuret
- positive test goes from blue to purple/lilac
describe function and structure of insulin
-plays a role in blood glucose regulation
-two polypeptide chains linked by disulfide bonds
-bind to specific receptor molecules e.g glycoprotein on outside of muscle and fat cells to increase uptake of glucose from the blood
describe the function and structure of pepsin
-one polypeptide chain, has many acidic R groups to withstand acidic conditions in stomach
-protein digesting enzyme to make amino acids made in the stomach
describe the function and structure of keratin
-contains very high proportion of cycteine so lots of disulphide bridges
-hydrogen bonding making it very strong
-skin hair and nails where it provides mechanical protection and impermeable barrier to infection and water