amino acids Flashcards
what is the monomer of proteins
amino acids
what is the structure of amino acids
H
H2N - C - C -ooh
R
what is the name of the bonds between amino acids
peptide bonds
how top peptide bonds form
oh of the carboxyl group and a H from the ch2 combine
what is primary structure
the sequence of amino acids in a protein
what is secondary structure
what binds hold it together
what are the 2 possible shapes
How the amino acid chain twists and bends \held together by hydrogen bonds
Alpha helix of beta pleated sheet
what is tertiary structure
when the coils and pleats themself start to fold and form shapes
disulphide bridges ionic bonds and hydrophobic/phyklic interactions
what is quaternary structure
how multiple protein chains combine
eg: haemoglobin is 4
what ionic bonding occurs in proteins
Ionic bonds can occur between those carboxyl and amino groups. NH3 + COO-
Hydrophobic and hydrophilic interactions in proteins
Hydrophobic parts of the R group tend to associate together in the centre of a chain to avid water. In the same way the opposite is true
Collagen P
provides mechanical strength
In arteries collagen prevents them from bursting
Tendons are made from collagen
Bones are made from collagen
Cartillage and connective tissue is also made from this
Keratin
Found in the body wherever hardness is essential
For example the disulphide bruges provide support for horns in goats and in our nails
Elasin
Cross lining and coiling makes this string and extensible
Skin can stretch back to its normal shape and around bones
Elastin in lungs allow them to stretch and return
Helps our blood vessels to stretch and recoil
Haemoglobin
4 polypeptide chains (2 alpha and 2 beta) each has its own tertiary structure
Each chain a haem group is stored. The protein is conjugated
The harm group allows haemoglobin to carry 02 in the blood
Insulin
2 polypeptide chains ( one alpha and one beat )
Hydrophylic r groups are on the outside of the molecule making it water and blood soluble