biochemistry Flashcards
(93 cards)
what are the functions of protein?
enzyme catalysts- e.g endonuclease .transport and storage e.g.heamoglobin .movement e.g.cytoskeleton .mechanical support e.g.collagen .immune protection .signalling and receptors .ion channels e.g. integral proteins in plasma membrane
what are proteins built from?
amino acids are the bricks that build protein.
what is the structure of amino acids?
central carbon that has 4 single covalent bonds to
.amine group -NH2
.carboxyl group- COOH
.H atom
.R group which varies and determines type of amino acid
how many amino acids are there?
there are 20 standard amino acids
what determines the difference between amino acids?
the R group varies between amino acids and determines the difference between these protein monomers.
what does the R group determine?
the R group determines the chemical nature of amino acids and their physical properties e.g.- the chemical nature .acidic- glutamate .basic- serine, tyrosine .non-polar- alanine, valine, leucine .polar- lysine, histidine, arginine physical nature -size
what is proline?
the R group covalently binds the carbon to the nitrgogen atom (amine group) folding back the amino acid forming a ring.
what is the property of proline?
proline has strong rigidity compared to other amino acids the rigidity of proline helps to stabilize folded proteins.
what is proline usually found?
often found in very tight turns in protein structures , where polypeptide chain must change direction.
what is the specialised property to proline?
proline can induce kinks into alpha helices due to its configuraation , since it is unable to adopt a normal helical conformation.
what is a peptide bond?
is it when the carboxyl group of one amino acid and the amine group of another amino acid covalently bind in a condensation reaction with water being formed
how is the protein shape dictated?
the protein shape will be dictated by the amino acid sequence
how is the polypeptide chain formed and stabilized?
the polypeptide chain folds into a shape (3D) which is stabilized by several non-covalent interaction.
.e.g hydrophobic so the chain would then twist inside and hide from the aqeuous environment outside .
what is the structure of amino acid in an aqueous environment?
polar amino acids tend to be located on the outside of the protein in an aqueous environment with non-polar amino acids on the inside
what are the types of bonds/non-covalent interactions to be aware of?
.ionic bonds
.hydrogen bonds
.van der waals interactions
what is a disulphide bond?
it is a covalent bond between a sulphur and sulphur.
what is unique about the disulphide bond?
R groups only covalentally bond if its sulphur
what is the folding pattern of proteins known as?
conformation
what are the two patterns that are predominate in proteins?
α-helix
β-pleated sheet
they are predominate in proteins because they efficiently fill space
what is the structure of an α-helix?
.rod like structure tightly coiled around a single polypeptide chain
. 4 amino acids to every 1 turn
.tightly coiled backbone forms the inner part of the rod and the R group extends outwards.
.stabilised by hydrogen bonds between NH2 and COOH group of main chain
what is the structure of β-pleated sheet ?
. formed by the linking of two or more beta strands (linear polypeptide chains)
.poly peptide chain fully extended allowing for more hydrogen bonds.
.adjacent stands can run parallel or anti parallel
.also stabilised by hydrogen bonds
and proline which creates a kink and then goes back on itself
what is a primary protein structure?
sequence of amino acid
what is a secondary protein structure?
α-helix and β-pleated sheet with folding as a result of hydrogen bonding between peptides
what is a tertiary protein structure?
3D conformation- folding of the poly peptide chain
- disulphide bonds form between the R group of α-helix and β-pleated sheet.