polymers and biochemstry
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addition polymer
forms when unsaturated monomers react to form a polymer Monomers contain C=C bonds
condensation polymerisation
there are two different monomers that add together and a small molecule is usually given off as a side-product e.g. H2O or HCl
Dipeptides
simple combination molecules of two amino acids with one amide (peptide) link
primary structure of proteins
is the sequence of the 20 different naturally occurring amino acids joined together by condensation reactions with peptide links
Secondary Structure: α-helix
The 3D arrangement of amino acids with the polypeptide chain in a corkscrew shape is held in place by Hydrogen bonds between the H of –Nδ- —Hδ+ group and the –O of Cδ+=Oδ- of the fourth amino acid along the chain
Secondary Structure: β-Pleated Sheet Structure of Proteins
The secondary structure can also take the form of a β– pleated sheets The protein chain folds into parallel strands side by side
Tertiary Structures of Proteins
folding of the secondary structure into more complex shapes. It is held in place by interactions between the R- side groups in more distant amino acids . These can be a variety of interactions including hydrogen bonding, Disulphide bridges and ionic interactions
Stereospecific active site
If the substrate is chiral then its likely that only one enantiomer will have the correct stereochemistry to fit in the active site of the enzyme and so only one isomer will be catalysed
inhibitor
will often bind to the active site strongly so stopping the substrate attaching to the enzyme
Catalyst
substance which speeds up the rate of reaction without being used up
cis platin
a complex of Pt(II) which is used as an anticancer drug
how does cisplatin work?
it prevents DNA replication in cancer cells by a ligand replacement reaction with DNA ( during this reaction a bond forms with platinum and nitrogen atom in guanine)
developing agents
used to locate amino acids on a chromatogram
enzyme
biological catalyst made of proteins and have stereospecifc active sites
nucleotide
molecule made from a phospate ion bound to 2-deoxyribose to one of 4 bases in DNA
peptide link
bond which forms between the carboxyl group (-COOH) of one amino acid and the amino group (-NH2) of another in a protein
TLC
technique used to identify compounds such as amino acids
how does TLC work?
uses a solvent and a plastic sheet coated in silica
active site
the region of an enzyme where the substrate binds
‘α’ amino acid
means both NH2 and COOH are bonded to the same C
are amino acids optically active ?
All amino acids, except glycine,are chiral because there are four different groups around the C. So they rotate plane polarised light.
what state do amino acids exist in ?
solid
what type of buffers can amino acids act as?
weak buffers
what allows amino acids to have high bp?
ionic interactions between zwitterions