post worksheet(s) Flashcards

1
Q

ta BLANK reaction involves the formation of covalent bonds and the creation of water

A

CONDENSATION

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2
Q

a BLANK type of bond is formed when two monosacharides combine to form a disacharide

A

glycocydic

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3
Q

homodimer

A

two of the same protein combined to make one large portein that does one function

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4
Q

homotetramer

A

four of the same protein combined to make one large protein that does one function

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5
Q

heterotetramer

A

protein made up of four smaller and different polypeptide chains

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6
Q

homotetramer

A

protein made up of four identical smaller proteins

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7
Q

what kind of bond is a disulfide bond?

A

covalent

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8
Q

2 ways enzymes are regulated

A

y non-covalent interactions with effector molecules and reversible covalent modifications, like phosphorylation

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9
Q

are peptide bonds IMFs?

A

no no no. only:
london forces
hydrogen bonds
electrostatic attraction
hydrophilic/phobic

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10
Q

A series of enzymes catalyzes reaction X - Y - Z - A. The enzyme Yoda converts X to Y. You suspect that product A may regulate Yoda’s activity, as you observe that Yoda’s activity decreases when
the concentration of A increases. Describe two ways in which product A may decrease Yoda’s activity.
Explain your answer.

A

the first way in which product A may decrease yoda’s activity would be if it was a competitive inhibitor of yoda. this would mean that product A and yoda were constantly competing for the active sit of product Z so the more product A that is produced, the more competition between the two competitors and activity level of yoda decreases due to this competition.

the second way in which product A could decrease yoda’s activity would be through allosteric inhibition. this would mean that product A was an allosteric (as opposed to competitive) inhibitor and that, when produced, it would stop yoda from being able to bond succesfully with X or Y (we dont know exactly how it catalizes the reaction) as the active site would be the wrong shape due to the presence of the bonded allosteric inhibitor

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11
Q

evidence for endosymbiosis

A
  1. double membrane
  2. ability to self reproduce
  3. its own dna
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12
Q

how to distinguish if an enzyme is being inhibited by allosteric or competitive inhibition

A

observe the bound enzyme and see if the compound is bound to the active site (same site as the substrate) or the allosteric site.

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13
Q

why is fermentation important to/for the cell?

A

the process of fermentation creates more NAD+ which is needed for glycolysis

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14
Q

two common ways to provide energy for active transport

A

ATP and Na+coupled

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15
Q

which stage of ‘digestion’ produces the most energy (ATP)

A

oxidative phosphorilation AT END

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16
Q

what makes a phospholipid more or less mobile?

A

double bonds (kinks) in phospholipids create more bends and flexibility in the phospholipid.

LESS carbons = MORE mobile
MORE double bonds = MORE mobile

17
Q

provide a classic example of a symport. name it and explain its function.

A

classec example of a symport is the glucose pump which moves glucose UP its concentration gradient and is able to do this by moving a Na+ ion in the same direction as the glucose but doen the Na+’s concentration gradient

18
Q

describe ATP synthase and explain both its function and how it functions

A

ATP synthase is an enzyme located on the inner mitochondrial membrane which harnesses the electrochemical gradient across this membrane to create ATP by allowing H+ ions to move down their electrochemical gradient (releasing energy) which spins a turbine-like structure which captures the released energy in order to fuse an inorganic phosphate to ADP, forming ATP

19
Q

do you need oxygen for…

the electron transport chain?
ATP synthase
anything functioning similarly to ATP synthase

A

yes!
yes!
yes!

electrochemical gradient used by ATP synthase is created by the electron transport chain which requires oxygen (otherwise fermentation happens)

20
Q

how much ATP does one NADH make

A

2.5 ATP

21
Q

how much ATP does one FADH2 make

A

1.5 ATP

22
Q

3 principle stages of immuno/western blot

A

electroblotting, immunoblotting, detection

23
Q

SDS-PAGE (in immunoblot)

A

denatured proteins are seperated by size (mass)

24
Q

steps of immuno/westerblotting

A
  1. denatured proteins are seperated by size and transfered to a seperate membrane
  2. antibodies are added to bind to specific protein(s)
  3. secondary antibodies are added which bind to primary ones and are often labeled (reporter enzymes) to be easily seen (change in color, light)
25
Q

sodium (Na+) - glucose transpoter

A

this is a symport.

one Na+ goes down it concentration grade ad the energy released from this energetically favorable reaction is used to bring the glucose along with the Na+ (up its concentration gradient) both the Na+ and glucose go through the transporter at the same time and one cannot go without the other

26
Q

snRNPs (function)

A

recognize intron sequence of nucleotides and binds to mRNA to cut out introns