Topic 1 - 1.24 Proteins :3 Flashcards
what monomers are proteins made up of
amino acids
what are groups are amino acids made up of
Carboxyl group (-COOH), amino group(NH2) and an R group(either glycine which is -H or cysteine which is CH2-SH)
what elements are proteins made of
nitrogen, oxygen, hydrogen, carbon and sometimes sulphur
How many naturally occurring amino acids are there
20
what is formed when 2 amino acids bond and what bond is formed
dipeptide, peptide bonds between carboxyl and amino acid
what other bonds except for peptide bonds can form between amino acids
depends on R group
disulfide, ionic and hydrogen bonds
Describe charges in an amino acid structure and how they help bonds form
the oxygen from the carboxyl group has a slightly negative charge while the hydrogen in the amino group has slightly positive charges.
this means they are attracted to eachother forming hydrogen bonds.
when and how do disulfide bonds form
when 2 cysteine molecules (R group) in a polypeptide are close together
oxidation reaction between 2 sulphur containing groups… strong covalent bond knows as a disulfide bond.
what protein structure are disulfide bonds usually present in
tertiary structure
What are salt bridges
ionic bonds between strongly positive and negative amino acid side chains
Describe the primary structure of a protein
linear sequence of amino acids in a polypeptide
> > helps determine final 3 dimensional shape of the protein molecule
Describe the Secondary structure of a protein
hydrogen bonds cause polypeptide to twist and fold into shape
examples-alpha helix or beta pleated sheets
Describe the tertiary structure of a protein
3 dimensional shape of a polypeptide chain
first folds into secondary structure(hydrogen bonds)
chain continues folding into tertiary structure
active site of enzymes depends on tertiary structure
Describe the quaternary structure of a protein
the three dimensional arrangement of more than one tertiary polypeptide
> > > shows how individual sub units are arranged to form a larger 3 dimensional structure.
Also shows us the position of any prosthetic group
Outline the structure of fibrous proteins and its properties
they have little/ no tertiary structure.
long parallel polypeptide chains, occasional cross linkages
insoluble in water+ very tough
found in connective tissue in tendons
keratin
matrix of bones