Biochemistry Flashcards
RNA (ribonucleic acid)
- mRNA carries a message from a gene in DNA to ribosomes for sequencing of amino acids in a protein
- uracil
- single stranded
- straight line
DNA (deoxyribonucleic acid)
- stores genetic info
- DNA gene codes for the order of amino acids in a protein
- thymine
- double stranded
- double helix
acidic solutions
-substances that ionizes in water, releasing hydrogen ions
basic solutions
-substances that ionizes in water, releasing hydroxide ions or take up hydrogen ions
ionic bonding
- metal with nonmental
- held together by an attraction between oppositely charged ions
- simple not complex
- inorganic
- when dissolved in water - breaks into ions
covalent bonds
- atoms share electrons
- in water breaks down into molecules
- large and complex because carbon is able to form 4 covalent bonds
- organic
glycogen
- stored in the liver and muscles
- when broken down into glucose molecules, they enter the blood and are transported to our cells to be used by cellular respiration
primary structure
- specific sequence of amino acids joined together by peptide bonds
- not functional protein
secondary structure
- primary structure can coil and form helixes, while other parts will zig zag upon itself and form pleated sheets
- hydrogen and peptide bonds hold the secondary structure together
- not functional protein
tertiary structure
- secondary structure folds upon itself to form a 3D globular structured protein that is functional
- held together by peptide bonds and disulphide bonds
quaternary structure
- occurs when two or more different polypeptides in their tertiary tertiary structure joint together
- functional protein
peptide bond
-covalent bond between the carbon from the carboxyl group and nitrogen from amino group
dehydration synthesis of a peptide
- hydroxyl group of the carboxyl group of an amino acid and a hydrogen atom from another amino acid enter a ribosome (acts as enzyme)
- ribosome removes hydroxyl group from one amino acid and the hydrogen atom from the amino group of the other amino acid
- hydroxyl group combines with the hydrogen atom to form water
- covalent bond forms (peptide bond) between carbon of the carboxyl group and nitrogen of the amino group
- dipeptide is formed
- anabolic
hydrolysis of peptide
- dipeptide enters enzyme peptidase
- peptidase breaks the peptide bond between carbon of carboxyl group and nitrogen from amino group
- water molecule splits into H+ and OH-
- OH- attaches to the carbon and H+ attaches to nitrogen to keep the 2 subunits apart
- 2 amino acids are formed
- catabolic
ATP (adenosine triphosphate)
- atp undergoes hydrolysis and energy is released
- produced by cellular respiration in the mitochondria
- some are produced in the cytoplasm
hydrogenation
- addition of hydrogen to an unsaturated fatty acid to convert it to a saturated fatty acid
- removes a double covalent bond and replacing it with a single covalent bond; this allows oils and processed foods to last longer on your self before it goes rancid
coenzymes
- organic non-protein cofactors
- vitamins are often compounds of coenzymes
(-molecules which help coenzyme function)
(-copper and zinc are examples of inorganic cofactors)
gastric or pancreatic protease
functional proteins -> polypeptides
pancreatic lipase
fats (triglyceride) -> glycerol and 3 fatty acids
DNA/RNA nuclease
nucleic acids -> DNA/RNA nucleotides
amino group
H, H, N
carboxyl group
O, C, OH
nucleotide structure
- phosphate
- pentose sugar
- nitrogen-containing base
- deoxyribosugar/ribosugar*
hydrogen bonding in water
-water is polar so it forms hydrogen bonds because hydrogen bonds form between a slightly H+ and a slightly O-
chemical reactivity-outer, energy level
- first shell can contain two electrons (duet rule)
- each additional shell can contain eight electrons (octet rule)
electrons
-negative charge
atomic number
- # of protons and electrons
glucose + glucose ->
maltose + water
glycerol + fatty acids ->
triglyceride (fat) + water
a2 + a2 ->
dipeptide
glucose + fructose ->
sucrose
competitive inhibitors
- attach to the enzyme in its active site
- when inhibitor and substrate are present, the two compete to occupy the active site
- when there’s lots of inhibitors it will occupy the active site blocking the substrate from binding, stopping enzyme activity
denaturation
molecular shape and structure are changed
catalyst
- chemical that speeds up a chemical reaction but is not used up in the reaction
- can be recovered and unchanged when reaction is complete
- function by lowering the amount of energy needed to initiate the reaction
lock and key
- enzyme physically fits with a specific substrate
- enzyme and the substrate joint together to form an enzyme-substrate complex
- in active site
induced fit
- active site is not a fixed arrangement but it’s flexible to allow a better fit
- active site changes shape to accommodate substance
