1.2 Flashcards
biological molecules 1
what bonds form the 3D structure of a protein
hydrogen bonds
disulfide bonds
ionic bonds
how do hydrogen bonds form in proteins
negative oxygen in the carboxylic acid and positive hydrogen in amino acid group important in folding and coiling
how do disulfide bonds form in proteins
two cysteine molecules close together
oxidation reaction creates covalent bond between two sulfur
stronger than hydrogen bond
needed to hold folding of amino acid chains
how do ionic bonds form in proteins
strongly positive and negative amino acid side chains form ionic bonds also known as salt bridges
explain the primary structure of protein
sequence of amino acids held by peptide bonds
explain the secondary structure of a protein
the arrangement of the polypeptide chain into a regular repeating structure held by hydrogen bonds
what is alpha helix structure
spiral coil
peptide bonds form backbone
R group stick out in all directions
what is the beta pleated sheet structure
regular pleats held by hydrogen bonds most fibrous proteins have this structure
explain the tertiary structure of proteins
level of 3D organization further folding into complex shapes held by hydrogen bonds, disulfide bonds, ionic bonds
e.g. globular proteins
which structure are fibrous & globular proteins
fibrous - secondary
globular - tertiary
explain the quaternary structure of a protein
3D arrangement of multiple tertiary poly-peptides and the addition of a prosthetic group
e.g. hemoglobin
what is the structure of a fibrous protein and give an example
little/no tertiary structure long parallel peptide chains occasional cross-linkages form fibers insoluble
e.g. collagen
state 5 uses of fibrous proteins
connective tissue in tendons
matrix of bones
structure of muscles
silk of spiderwebs
silk worn cocoons
keratin
explain the structure of collagen and what it’s used for
strengths tendons, bones, ligaments & skin
3 poly peptide chains each about 1000 amino acids
triple helix held by hydrogen bonds, found together in fibrils
what structure do globular proteins have
tertiary & sometimes quaternary
why do globular proteins not dissolve in water
they are too big so instead form a colloid
why are globular proteins important
hold molecules in position in the cytoplasm
forms enzymes & hormones
what type of proteins are red blood cells
globular & conjugated
what is a conjugated protein
a protein which is joined with a prosthetic group
what prosthetic group does a red blood cell have
iron
what are glycoproteins
proteins with a carbohydrate prosthetic group
what are the properties of glycoproteins
they hold onto a lot of water so it is harder for them to be broken down
very slippery & viscous
give an example of a glycoprotein
mucus
synovial fluid
what are lipoproteins
proteins conjugated with lipids
why are lipoproteins important
transport of cholesterol - lipid prosthetic group enables it to combined with the lipid cholesterol
how big are LDLs (low density lipoproteins)
22nm
how big are HDLs (high density proteins) and why do they have a higher density
8-11nm
contain more protein