topic 1.3 - proteins Flashcards
primary structure of a protein
sequence of an amino acids that make up the polypeptide chain
secondary structure
can either be alpha helix or beta pleated sheet
what is the sequence of a protein determined by
the DNA of the gene that encodes the protein. Even changing just one amino acid in a protein’s sequence can affect the proteins overall structure and function
importance of insulin and glucagon as proteins
control blood glucose concentration
how is an α-helix formed
due to hydrogen bonds forming between the oxygen of -CO group of one amino acid and the hydrogen of the -NH group of the amino acid 4 places ahead of it
how is a β-pleated sheet formed
two or more segments of a polypeptide chain line up next to each other forming a sheet like structure held together by hydrogen bonds
tertiary structure
folding of the protein in order to form a precise 3D shape
bonding in a tertiary structure
- hydrogen bonds : formed between polar groups like -NH, -CH, -OH groups (broken & reform by change in temp or pH)
- disulfide bonds : formed between two cysteine molecules which are close in strcuture of a polypeptide. Much stronger than hydrogen bonds as it is covalent. (broken by reducing agents)
- ionic bonds : between ionised amine (NH3+) and ionised carboxylic acid (COO-)
quarternary structure
proteins are made up of two or more polypeptide chains
held together by hydrogen bonds, disulphide bonds & ionic bonds
globular proteins
- proteins that curl up into a ball shape so their hydrophobic groups are in the centre while the hydrophilic groups remain on the outside and relate well to the blood
- enzymes
fibrous proteins
- molecules do not curl up
- not soluble in water
- role is mostly structural
- e.g. collagen, keratin
globular protein - haemoglobin
- carries oxygen and found in red cells
- 4 polypeptide chains
- each polypeptide chain is called a Globin held together by disulfide bonds
- each chain is arranged around a haem group (contains iron)
- iron enables haemoglobin to bind to and release oxygen molecules
- when haemoglobin binds to oxygen it is bright red, when there is no oxygen it is blue/purple
fibrous protein - collagen
- most common protein found in animals
- not folded; form strands
- insoluble as it provides a structural function
- 3 polypeptide chains arranged in a triple helix held together by hydrogen and covalent bonds
advantages of collagen
- flexible
- high tensile strength so not easy to break when pulled