T1 M2 Organelles, Energy and App lec Flashcards

1
Q

oxidative phosphorylation

A

using oxygen as the final electron carrier in the ETC, resulting in the production of water

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2
Q

substrate-level phosphorylation

A

synthesis of ATP by adding a phosphate group to an ADP molecule

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3
Q

endomembrane system

A
  • present in eukaryotic cells
  • incl the nuclear envelope, and other membrane structures such as the ER, golgi apparatus and plasma membrane surrounding the cytoplasm
  • perform most lipid and protein synthesis
  • allows for phagocytosis and exocytosis which involve compartmentalization of things entering and exiting the cell
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4
Q

are chloroplasts and mitochondria included in the endomembrane system?

A

no because they are likely bacteria that were engulfed by eukaryotes over time and evolved to develop their present function
- also they have their own DNA

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5
Q

prokaryotic cells

A

unicellular organisms lacking a nucleus and have few to no organelles

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6
Q

eukaryotic cells

A

organisms whose cells contain a nucleus and many membrane bound organelles

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7
Q

photosynthesis

A

process used in plant cells to convert light energy into chemical energy that will get stored in the bonds of carbohydrate molecules
- happens in double membraned chloroplast

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8
Q

cellular respiration

A

process used in plant and animal cells to release energy stored in bonds of carb molecules and form ATP
- happens in double membraned mitochondria

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9
Q

about how many mitochondria are there in a cell?

A

anywhere from 50 to 1,000,000

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10
Q

how are mitochondria similar to bacteria

A
  • they have their own circular genome
  • produce enzymes necessary for protein synthesis
  • about same size and appearance as bacterial cells
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11
Q

endosymbiotic theory of organelle evolution

A

states that early eukaryotes became hosts to aerobic and photosynthetic prokaryotes which we now know as mitochondria and chloroplasts
– these temporary relationships are permanent and heritable thus they are part of the cell now

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12
Q

why are organelles important?

A
  • they allow for compartmentalization. ie certain enzymes w like functions can be kept together
  • also opposing functions can be kept separate
  • increases membrane surface area
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13
Q

increased membrane surface area can cause what?

A
  • increases potential metabolic capacity across the membrane
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14
Q

glycosidic linkages

A

covalent bonds formed b/w monosaccharides (condensation reactions) to form complex sugars
- give alpha or beta 1, 4 glycosidic linkages b/w OH groups on C1 and C4 molecules

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15
Q

name the monosaccharides

A

glucose
fructose
galactose

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16
Q

name the disaccharides

A

sucrose
lactose
maltose

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17
Q

polysaccharides

A

often storage from of energy

starch and glycogen

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18
Q

ETC

A

electron transport chain
- present in inner mitochondrial membrane
establishes a proton gradient used to produce ATP in mitochondria yields 36 ATP/ 32 idk hopefully this isn’t a question

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19
Q

how many ATP are yielded from a molecule of glucose

A

30

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20
Q

exergonic reaction

A

produces energy

ex. hydrolysis of ATP

21
Q

ATP

A

composed of 3 phosphate groups, a ribose sugar and an adenine
- cleavage of a phosphate group yields 30.5 kJ/mol ATP

22
Q

oxidation and reduction reaction

A

reduction: gaining e-
oxidation: losing e-

23
Q

beta oxidation of FAs

A

allows fatty acids from lipids to be broken down into NADH and FADH2 and Acetyl CoA to yield energy

24
Q

when sufficient carbohydrate is not present, the body will use what as energy?

A

lipids first, then proteins
glycerol -> glucose and enters cycle
AAs -> pyruvate -> TCA

25
Q

the camel’s hump

A
  • can weigh up to 80 lbs
  • consists of pure fat (tristearin - lots of bonds can be broken to yield plenty of energy, also a source of water bc produces H2O when metabolized)
  • size increases when replenishes food source and decreases when camel goes w/o eating for a long time
  • camels have extreme water loss tolerance (30-40% is ok), long noses to keep moist air, dry feces
26
Q

migrating geese

A

eat a lot in fall, to have enough energy to migrate, they can lose up to half of their entire body weight in fat

27
Q

what is the most extreme bird

A

bar headed goose
- flies over mountains at high speeds – 65km/h
they break down FAs into bloodstream and proteins carry them to muscle cells where there are more mitochondria
- also have greater ventilation rates w thinner alveolar membranes at capillary beds w lots of mitochondria, Hb binds to O2 better

28
Q

locusts

A

can fly over oceans

- start by breaking down glucose and after 30 mins begin using lipid stores as energy

29
Q

ketone bodies

A

contain 38% more recoverable energy than glucose and FAs as they can be converted into acetyl coA
- are these an alternative source of fuel?
they are produced when more FAs circulate in the body

high ketone drink called delta G given to athletes can provided higher degree of energy.
is this doping? this is expensive. are there side effects?

30
Q

some functions of proteins

A
  • transport and signalling: hormones, protein channels
  • movement and structure: myosin, actin
  • enzymes
  • defense: antibodies
31
Q

nucleus

A

double membrane bound domain that contains chromosomes which pack and control DNA molecules, contains most of the genes in a eukaryotic cell

32
Q

nucleolus

A

a non membrane bound spherical structure within the nucleus that contains the genes and transcripts for rRNA

33
Q

nuclear pores

A

allow for things to move between nucleus and cytosol such as nucleic acids and enzymes

34
Q

ribosomes

A

synthesize proteins
2 kinds produce diff kinds of proteins
- also remain free in cytoplasm or attached to ER until needed

35
Q

condensation reactions that polymerize amino acids are where

A

catalyzed within the ribosome

36
Q

chemical structure of a protein/ amino acid

A

central carbon w a H, amino group and carboxyl group

also a variable side chain connected to central C gives protein unique properties

37
Q

peptide bonds

A

bonds b/w amino acids that are made via condensation reactions and result in formation of polypeptides
- form b/w OH group and amino group of 2 AAs

38
Q

what is important about the properties of the side chain in a protein?

A

they dictate the shape of a protein

ie hydrophobic will slide inside and hydrophilic stays outside

39
Q

primary protein structure

A

sequence of AA formation

40
Q

secondary protein structure

A

folding into alpha helix or beta pleated sheet

41
Q

alpha helix protein folding

A

polymer is turned into a spiral by formation of H bonds b/w carbonyl and carboxyl groups
- R groups stick out from helix

42
Q

beta pleated sheet protein folding

A

broad lines w arrowheads made of parallel protein strands w H bonds also formed b/w carboxyl and amino groups of adjacent strands

  • R groups extend above and below the B-sheet
  • adjacent strands can run in opposite (antiparallel) or the same (parallel) direction
43
Q

tertiary protein structure

A

3-D shape forms that will determine function

- determined by interactions b/w R groups

44
Q

free ribosomes

A

translate proteins that will remain in the cytosol or be targeted to organelles that include the nucleus, mitochondria and chloroplasts
- some of these proteins incl enzymes for glycolysis, or structural proteins

45
Q

what are some interactions b/w R groups that occur

A

H bonding, Van der Walls interactions, covalent and ionic bonding, disulphide bonding and hydrophobic interactions

46
Q

quaternary protein structure

A

association of different polypeptide subunits to form a fully functional protein

47
Q

molecular chaperones

A

proteins that bind to hydrophobic regions of nascent polypeptides and prevent incorrect folding long enough for the correct structure to form

48
Q

chaperonins

A

large molecular complexes that form isolation chambers

- nascent proteins are held here so it doesn’t interfere with proper protein folding