amino acids, proteins and DNA Flashcards
at nuetral pH and in solid state amino acids exist as
zwitterions
H from COOH removed so COO- and added to NH2 forming +NH3
structure of amino acid
H2N-CHR-COOH
at low pH amino acids exist as
+NH3-CHR-COOH gained h has more acidic
at high pH amoni acids exist as
NH2-CRH-COO- as more alkaline so loses H
proteins are
condensation polymers of amino acids joined by peptide links
the importance of hydrogen bonding and disulphite bonds in proteins
hold proteins in shape ,
hydrogen bonding exist between polar groups(-OH and -NH2) stabilize the secondary and tertiary structure of protein
disulphite bonding between cysteine, link diff part of protein chain together help to stabilise the tertiary strucutre
primary structure of protiens
number and order of amino acids in polypepetide chain
seconday structure of protiens
peptide links form hydrogen bonds with each other resulting in alpha helix or beta pleated sheets
tertiary structure of proteins
3D tertiary structure
disulphite bonds
hyrogen bonds
ionic bonds
hydrolysis of the peptide link produces
the constituent amino acids
how can amino acids be sperated and identified
thin layer chromotgraphy
used developing agents such as ninhydrin or UV light to locate then caluculate Rf values
enzymes are
proteins
action of enzymes as catalysts
substrate fit exactly into the active site that is stereospecific so only bond to one enantiomer of a substrate.
enzyme substrate complex forms reducing the Ea to break bonds within the molecule and catalyses’ the reaction
principle of a drug acting as an enzyme inhibitor
similar shape to sunstrate so compete with the substrate to bond to the active site but no reaction follows instead they block the active site so no sunstrate can fit in
how can drugs’ acting as enzymes inhibitor be deigned
computers
if an undesirable biological process occurs which is catalyzed by and enzyme a computer is used to determine the shape of an active site and design another molecule that will fit into the active site (must be correct enantiomers)