Biochemistry Flashcards

(36 cards)

0
Q

RNA (ribonucleic acid)

A
  • mRNA carries a message from a gene in DNA to ribosomes for sequencing of amino acids in a protein
  • uracil
  • single stranded
  • straight line
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1
Q

DNA (deoxyribonucleic acid)

A
  • stores genetic info
  • DNA gene codes for the order of amino acids in a protein
  • thymine
  • double stranded
  • double helix
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2
Q

acidic solutions

A

-substances that ionizes in water, releasing hydrogen ions

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3
Q

basic solutions

A

-substances that ionizes in water, releasing hydroxide ions or take up hydrogen ions

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4
Q

ionic bonding

A
  • metal with nonmental
  • held together by an attraction between oppositely charged ions
  • simple not complex
  • inorganic
  • when dissolved in water - breaks into ions
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5
Q

covalent bonds

A
  • atoms share electrons
  • in water breaks down into molecules
  • large and complex because carbon is able to form 4 covalent bonds
  • organic
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6
Q

glycogen

A
  • 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
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7
Q

primary structure

A
  • specific sequence of amino acids joined together by peptide bonds
  • not functional protein
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8
Q

secondary structure

A
  • 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
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9
Q

tertiary structure

A
  • secondary structure folds upon itself to form a 3D globular structured protein that is functional
  • held together by peptide bonds and disulphide bonds
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10
Q

quaternary structure

A
  • occurs when two or more different polypeptides in their tertiary tertiary structure joint together
  • functional protein
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11
Q

peptide bond

A

-covalent bond between the carbon from the carboxyl group and nitrogen from amino group

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12
Q

dehydration synthesis of a peptide

A
  • 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
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13
Q

hydrolysis of peptide

A
  • 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
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14
Q

ATP (adenosine triphosphate)

A
  • atp undergoes hydrolysis and energy is released
  • produced by cellular respiration in the mitochondria
  • some are produced in the cytoplasm
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15
Q

hydrogenation

A
  • 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
16
Q

coenzymes

A
  • organic non-protein cofactors
  • vitamins are often compounds of coenzymes

(-molecules which help coenzyme function)
(-copper and zinc are examples of inorganic cofactors)

17
Q

gastric or pancreatic protease

A

functional proteins -> polypeptides

18
Q

pancreatic lipase

A

fats (triglyceride) -> glycerol and 3 fatty acids

19
Q

DNA/RNA nuclease

A

nucleic acids -> DNA/RNA nucleotides

20
Q

amino group

21
Q

carboxyl group

22
Q

nucleotide structure

A
  • phosphate
  • pentose sugar
  • nitrogen-containing base
  • deoxyribosugar/ribosugar*
23
Q

hydrogen bonding in water

A

-water is polar so it forms hydrogen bonds because hydrogen bonds form between a slightly H+ and a slightly O-

24
chemical reactivity-outer, energy level
- first shell can contain two electrons (duet rule) | - each additional shell can contain eight electrons (octet rule)
25
electrons
-negative charge
26
atomic number
- # of protons and electrons
27
glucose + glucose ->
maltose + water
28
glycerol + fatty acids ->
triglyceride (fat) + water
29
a2 + a2 ->
dipeptide
30
glucose + fructose ->
sucrose
31
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
32
denaturation
molecular shape and structure are changed
33
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
34
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
35
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