pack 1 - Proteins Flashcards
structure and types
what 4 groups does a protein always contain
carboxyl group
amine group
R group (residual)
hydrogen
what reaction forms a dipeptide
condensation reactions
what bonds form
peptide bonds
where do the bonds from
between the amine group of one amino acid and the carboxyl group of another amino acid.
what reactions breaks peptide bonds
hydrolysis
describe the primary structure
specific sequence of amino acids in a polypeptide chain is formed by peptide bonds in a condensation reaction
describe the secondary structure
bonds from between amine and carboxyl group
form an alpha helix or beta pleated sheet
describe the tertiary structure
fold into a specific 3D shape which allows it to carry out its specific functions. held together by R groups
describe the quaternary structure
3D containing more than one polypeptide chain
what bonds from in tertiary and quaternary structure
hydrogen
ionic
disulphide
what bonds from in the secondary structure
hydrogen
structure of a fibrous protein
long and linear
little/no tertiary structure
hydrophobic R groups on outside- insoluble
structure of a globular protein
fold into a spherical shape
have tertiary structure (some quat)
hydrophilic R groups on outside- soluble
examples of fibrous proteins
fibrin
collagen
keratin
examaples of globular proteins
enzymes
thrombin
fibrinogen
haemoglobin
Fibrous protein riole
structural role in organisms
globular proteins role
role in metabolic reactions
how many polypeptide chains in haemoglobin
4
function of haemoglobin
bind to oxygen to be carried around the blood
how structure helps function of haemoglobin
- globular spherical structure = allows more haemoglobin to fit in each red blood cell
- form a conjugated protein = allow haem group to be held in correct position to bind to oxygen
- hydrophilic R group on outside = soluble to dissolve in cytoplasm of red blood cells
structure of haemoglobin
compact sphere- globular protein
tertiary structure- ionic hydrogen and disulphide bonds
hydrophilic chains on outside
conjugated protein- each polypeptide is associated with a iron haem group
collagen structure
fibrous protein
3 polypeptide chains wrap around each other- hydrogen and disulphide bonds-triple helix
staggered- collagen fibril- prevent weak points
cross links between molecules
how collagen structure aids function
hydrophobic R groups on outside- insoluble so in BV blood cannot diffuse out
triple helix- give strength
staggered in a fibril- high strength and flexibility without stretching. required in skin, bones. artery walls
what is a conjugated protein
proteins with another non protein group
(prosthetic) associated with their polypeptide chains