Protein structure and function Flashcards
Haemoglobin
Trasnports oxygen in blood
Alpha amylase
Breaks down starch within saliva
Collagen
Builds structures in mucsle and skin
Membrane bound ATP synthase
Lines inner membrane
DNA helicase & RNA polymerase
assist in transcription
trna
assist in translation
Amino acids components
Side chains dictate properties
Made of carbon, oxygen, hydrogen, nitrogen
Non polar amino acids
Hydrophobic properties
Polar amino acids
Hydrophilic properties
Primary protein structure
Sequence of amino acids - Polypeptide chain reading from N to C terminus
Residue
Monermic unit of polypeptide - Lyseine
Secondary structure
Amino acid sequence undergone localised folding held together by hydrogen bonds - Alpha and Beta
Alpha helix
Backbones form sprials with four amino acids per turn - Secondary structure
Beta sheets
One backbone faces one way, and u turns into opposite direction
Tertiary structure
Organised folding of protien with hydrophobic residues pointing inward and hydrophilic pointing out - Forms 3d structure of protien
Globular protiens structure
Tight, compact round blob
Fibrous protiens structure
Long, elongated and spindly
Quaternary structure
Mulitple polypeptide chains bonded together
Inhibitors
Prevent susbtrate entering enymes active site
Hydrogen bonds
Form backbone of protiens and folding
Weak bond but many
Electrostatic interactions
Salt/ionic bridge between two oppositely charged groups
Hydrophobic interaction
Clustering of polar and hydrophobic side chains away from water
weakest bond but most plentiful
Covalent bond
Strongest bond that occyrs spontaneously in oxidising conditions - Disulphide bond
Denaturation factors
ph
salt conc
temperature
Heat denaturation
Health makes protiens insoluble making them unravel and lose shape or form random bonds
Salt denaturation
Salt binding to a charged side chain can break electrostatic interactions
