polymers of life

central carbon surrounded by a hydrogen group, a carboxyl group, variable group and amine group

condensation polymers

by hydrolysis reflux with moderately concentrated hydrochloric acid- hydrolysing the C-N bonds

hydrolyse the protein under reflux then use chromatography to separate compare Rf values to known data base

the order of amino acid residues

the alpha coiling and formation of beta pleated sheets of the chain held together by hydrogen bonds between peptide links- between -NH and -C=O

the final folding determining the 3D shape f the protein intemolecular bonds, ionic bonds and covalent bonds. IDID between non polar R-groups hydrogen bonds between polar R-groups ionic bonds between ionisible R-groups covalent bonds between sulfur containing R-groups on cysteine residues to form disulphide bridges

made of a phosphate, sugar and a base

DNA has deoxyribose sugar, RNA has ribose sugar

phosphate units join by condensation with deoxyribose or ribose

join by condensation with the deoxyribose

2

3

hydrogen bonds break between the DNA strands bases of free nucleotides pair with complementary bases on nucleotides of DNA - ensures correct nucleotides join in correct place DNA polymerase joins sugar phsophate backbone of new chain results in 2 identical molecules, the same as the starting molecules

DNA helix unwinds to reveal a single stranded portion the DNA bases attract free RNA nucleotides with complementary bases the RNA nucleotides are joined together by RNA polymerase = mRNA the DNA coils up again mRNA is released to move arounds cell

ribosome attaches to mRNA at start codon tRNA with correct anticodon bases pairs with start codon inside the ribosome ribosome moves onto next triplet and different tRNA to bring next amino acid that the mRNA codes for the two amino acids join by a peptide bond the ribosome moves forward again and first tRNA breaks off from amino acid and next amino acid joins by the tRNA continues until stop codon

the part of a drug that fits into the receptor site and makes it medicinally active

size - particular size to fit into receptor shape - particular shape to fit into the receptor bond formation - functional groups in pharmocaphores form temporary bonds with functional groups in the receptor orientation- if pharmocaphore is E/Z optical isomer then only one will fit

at low concentrations of substrate, the order with respect to substrate concentration is one and rate increases as substrate increases however at higher concentrations of substrate the order with respect to substrate is zero as all active sites are in use for catalysis and substrate conc no longer has an effect on rate

redox reaction, forming carboxylate salt and hydrogen gas

carboxylate salt, carbon dioxide, water

neutralisation, forming carboxylate salt and water

a compound with a positive and a negative charge on it

normal amino acid structure but with a coo- isntead of carboxyl group and NH3+ instead of NH2