Molecules and Proteins Flashcards
(23 cards)
What is a Macromolecule?
large, biologically important molecules inside cells
What are macromolecules generally?
sugars, lipids, amino acids,
Is ATP a macromolecule?
no ATP is a nucleotide
What are oligosaccharides?
3-12 monosaccharides, products of polysaccharide digestion, part of lipid complexes
What causes monosaccharides to form ring structures?
often caused by reaction of the aldheyde/ketone group reacting with the hydroxyl group from the same molecule
3 parts of a fatty acid?
Methyl group, carbon chain, carboxyl group
Does raising the degree of unsaturation increase or decrease melting point of fatty acids?
more unsaturated (more double bonds) causes more kinks, so melting point decreases.
What format are double bonds shown in?
(18:1) so for every 18 carbons there is one double bond.
often shown as delta^first time double bond appears.
What are phosphoacylglycerols?
derived from phopshatidic acid. formed from fatty acids esterified to glycerol and phosphorylated at C3.
What are Sphingolipids?
derived from ceramide. (serine, palmitic acid and another fatty acid)
What are steroids made of?
made of cholesterol.
What are steroids used for?
emulsify fatty acids to form micelles
Where is cholesterol produced?
produced by the liver, absorbed by the gut.
5 points about peptide bonds?
very stable. cleaved by proteolytic enzymes. Partial C-N bond. Flexible around C atoms not involved in the bond. usually have one preferred form.
what forces hold proteins together?
Peptide bonds, hydrogen bonds, disulphide bonds, Van der Waals, ionic bonds, hyrophilic/phobic interactions
Secondary structures?
Alpha Helix: H-bonds between carbonyl groups and the N-H four amino acids down the chain.
Beta-Sheet: H-bonds between linear regions of polypeptide chains. can be parallel or antiparallel, pleated or not pleated.
What are some super-secondary structures?
beta-alpha-beta units, helix-turn-helix conformation, zinc fingers.
What is and causes tertiary structure?
the overall 3D conformation of a protein.
caused be electrostatic, hydrophilic/phobic, H-bonds and covalent interactions.
can change based on pH
What is Quartenary structure?
3D structure of a protein made of many subunits
What are isoenzymes?
enzymes who have different structures and sequences but catalyse the same reaction as another
What are coenzymes?
complex organic structures that help to maximise the repertoire of enzymes function groups.
What do activation-transfer coenzymes do?
form a covalent bond and are regenerated at the end.
what do oxidation-reduction coenzymes do?
involved in electron transfer reactions.
