Molecular Biology; Cellular Respiration Flashcards

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1
Q

lipid solubility

A

low solubility in water, high solubility in nonpolar organic solvents

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2
Q

amphipathic

A

polar and nonpolar

phospholipids - polar at phosphate end, nonpolar at fatty acid end

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3
Q

steroids

A

four ringed structures, some hormones, vitamin D, cholesterol, membrane component
regulate metabolic activities

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4
Q

phospholipids serve as …

A

structural component of membranes

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5
Q

triacylglycerols ….

A

store metabolic energy, provide thermal insulation and padding

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6
Q

some fatty acids serve as ____

A

local hormones

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7
Q

proteins = amino acids linked by

A

peptide bonds (also called polypeptides)

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8
Q

essential amino acids

A

body cannot make, have to be consumed

10 for humans

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9
Q

amino acids differ from each other only in their ___

A

side chains, R group

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10
Q

protein primary structure

A

number and sequence of amino acids

all proteins have primary structure

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11
Q

secondary structure of protein

A

alpha-helix or beta-pleated sheets
reinforced by H-bonds between the carbonyl oxygen and the hydrogen on the amino group
contribute to conformation of protein
most proteins have secondary structure

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12
Q

protein tertiary structure and 5 forces that create it

A

3D shape formed when the peptide chain curls and folds

  1. covalent disulfide bonds between 2 cysteine aas
  2. electrostatic (ionic) interactions
  3. hydrogen bonds
  4. van der Waals forces
  5. hydrophobic side chains pushed away from water toward the center of protein
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13
Q

Quaternary protein structure

A

when two or more polypeptide chains bind together

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14
Q

denatured protein

A

when conformation is disrupted

lost most of its secondary, tertiary, and quaternary structure

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15
Q

force disrupted from area (denaturing agent)

A

hydrogen bonds

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16
Q

protein structural force disrupted from salt or change in pH

A

electrostatic bonds

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17
Q

protein structural force disrupted from mercaptoethanol

A

disulfide bonds

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18
Q

protein structural force disrupted from organic solvents

A

hydrophobic forces

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19
Q

protein structural force disrupted from heat

A

all forces

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20
Q

when you see nitrogen in a structure…

A

think protein

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21
Q

anomers

A

stereoisomers of a cyclic saccharide that differs only in its configuration at the anomeric carbon
ring form of glucose has 2 anomers

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22
Q

if cell has sufficient ATP, glucose is polymerized to ____

A

glycogen (branched branched glucose polymer with alpha linkages)
large amounts in muscle and liver

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23
Q

plants form ___ and ___ from glucose

A

starch and cellulose (beta linkages - cant digest)

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24
Q

in absence of insulin, only the ___ and ___ continue to absorb glucose

A

brain and liver

25
Q

3 components of nucleotides

A

five carbon sugar, nitrogenous base, phosphate group

26
Q

bonds in nucleotides

A

phosphodiester bonds between phosphate group and 3rd carbon of pentose

27
Q

cyclic AMP

A

important component in many secondary messenger systems

28
Q

minerals

A

dissolved inorganic ions inside the outside the cell

29
Q

enzymes are typically ___ ____

A

globular proteins

30
Q

enzyme function

A

act as a catalyst (lowering activation energy, increasing rate of reaction)

31
Q

enzymes do not alter the ____ of a reaction

A

equilibrium

32
Q

lock and key theory

A

example of enzyme specificity

active site has specific shape that only fits a specific substrate

33
Q

induced fit model

A

shape of enzyme and substrate are altered upon binding, increases specificity and helps reaction proceed f

34
Q

saturation kinetics

A

as relative concentration of substrate increases the rate of the reaction also increases, but to a lesser and lesser degree until max rate has been achieved

35
Q

cofactor

A

non-protein component that many enzymes need to reach optimal activity
coenzymes (vitamins and derivatives) or metal ions/minerals

36
Q

irreversible inhibitors

A

bind covalently to enzymes and disrupt their function, highly toxic

37
Q

competitive inhibitors

A

compete with the substrate by binding reversibly with noncovalent bonds to the active site

38
Q

noncompetitive inhibitors

A

bind noncovalently to an enzyme at a spot other than the active site and change the conformation of the enzyme

39
Q

zymogen or proenzyme

A

inactivated form of enzymes

when specific peptide bonds are cleaved –> zymogens activated

40
Q

allosteric interactions/regulation

A

modification of enzyme configuration from binding of an activator or inhibitor at a specific binding site on the enzyme

41
Q

negative feedback/feedback inhibition

A

one of the products downstream in a reaction series comes back and inhibits the enzymatic activity of an earlier reaction

42
Q

positive feedback

A

product returns to activate the enzyme

occurs less often than negative feedback

43
Q

positive and negative cooperativity

A

first substrate changes the shape of the enzyme allowing other substrates to bind more easily = positive

44
Q

lyase vs. ligases

A

ligase requires energy from ATP or other nucleotide

45
Q

kinase vs. phosphatase

A

kinase: phosphorylates something
phosphatase: dephosphorylates something

46
Q

metabolism

A

all cellular chemical reactions
anabolism - molecular synthesis
catabolism- degradation

47
Q

respiration

A

energy acquiring stages of catabolic metabolism
oxidation to acetyl CoA, pyruvate etc.
citric acid cycle

48
Q

glycolysis

A

first stage of anaerobic and aerobic respiration
6C glucose –> 2 3C pyruvate + 2ATP + phosphate + water + 2 NADH
occurs in cytosol
2 ATP by substrate level phosphorylation

49
Q

substrate level phosphorylation

A

formation of ATP from ADP and inorganic phosphate using the energy released from the decay of high energy phosphorylated compounds as opposed to using the energy from diffusion of ions down their concentration gradient (as with oxidative phosphorylation)

50
Q

fermentation

A

anaerobic respiration

glycolysis, reduction of pyruvate to ethanol or lactic acid, oxidation of NADH to NAD+

51
Q

for aerobic respiration, products of glycolysis (pyruvate and NADH) move _____

A

into the matrix of a mitochondrion

52
Q

pyruvate converted to ___ once inside the matrix

A

acetyl CoA

produces NADH and CO2

53
Q

Kreb’s cycle/citric acid cycle

A

each turn produces 1 ATP, 3 NADH, 1 FADH2

54
Q

ATP production in Kreb’s cycle through

A

substrate level phosphorylation

55
Q

proton-motive force

A

proton gradient generated by ETC

propels protons through ATP synthase

56
Q

production of ATP with ATP synthase and proton motive force is ____

A

oxidative phosphorylation

57
Q

aerobic respiration produces about ____ net ATPs

A

36

58
Q

1 NADH brings back ____ ATPs

A

2 to 3

59
Q

1 FADH1 bring back ___ ATP

A

2