TEST 1 MATERIAL Flashcards

(35 cards)

1
Q

What are the 7 functions of proteins?

A

1: Enzyme catalysis
2: Defence
3: transport
4: support
5: regulation
6: motion
7: storage

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2
Q

What are the components of an amino acid? What is the role of each group?

A
  • Carboxyl group
  • Amino group
  • R group

The carboxyl and amino groups have the function of binding to each other to create a protein backbone
The R group influences different molecular interactions for different functions

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3
Q

What are the types of amino acids and which intermolecular interactions take place in each type?

A
  • non-polar, hydrophobic exclusion/van der waals
  • polar uncharged, H-bonding, cysteine can make a disulfide bridge
  • charged, ionic bonds
  • aromatic (special character)
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4
Q

What are the levels of protein organization? name and describe them

A

Primary: the sequence of amino acids present in the protein (Thr-Cys …).

Secondary: the molecular interactions between the back bone (H bonding) to form beta pleated sheets or alpha helices.

Tertiary: R GROUP

Quaternary: interactions between different polypeptides

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5
Q

How are amino acids numbered and why?

A

the N-terminus is always #1, because it is always added to the C terminus.

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6
Q

What characteristic do phospholipids have that allows them to form membranes? What in the chemical composition of phospholipids explain this characteristic?

A

They are half hydrophilic, and half hydrophibic due to the difference in polarity in the hydrophobic, non polar tail and the hydrophilic polar head.

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7
Q

What shapes do phospholipids arange themselves in? How do these phospholipids move in these shapes?

A

Phospholipids form bilayers, they can swing rotate, undergo transversal diffusion, or lateral diffusion

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8
Q

How does saturation of a phospholipid affect membrane fluidity?

A

If a phospholipid is unsaturated, it contains cis double bonds which cannot move freely, thus introducing a chink into the bilayer, creating more space between the phospholipids, increasing membrane fluidity

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9
Q

How do organisms influence membrane fluidity?

A
  • animals can introduce cholesterol as a supporting molecule to fill the holes in a membrane and make it more rigid
  • other organisms without cholesterol use enzymes to introduce double bonds in the membranes to counter effects of cold
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10
Q

What are the components of a membrane, and what are their functions?

A
  • Phospholipid bilayer, provides selectively permeable bilayer, excludes polar molecules like water, etc.
  • interior protein network, reinforces membrane shape
  • cell surface markers, allows identification of cells and identifying foreign organisms
  • transmembrane proteins, many uses, transport, enzymes, cell surface reception, cell identification, cell adhesion, attachement to cytoskeleton,
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11
Q

What are the types of tansmembrane proteins and what is their function?

A

transporters: carrying/allowing molecules to diffuse that cannot span the membrane

Enzymes: can be anchored to a membrane, catalyse chemical reactions

Cell surface receptors: allows molecules outside to transmit signal inside a cell

Cell surface identitiy markers: allows other cells to identify cells

Cell to cell adhesion molecules: sticks cells together

Attachment to the cytoskeleton

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12
Q

What is a concentration gradient? Which direction do molecules go?

A

two areas with different concentrations will to even out, thus molecules travel from high to low concecntration

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13
Q

what are the types of transport, through structure does the compound go, and in what direction?

A

simple diffusion: membrane, same as conc. gradient

facilitated diffusion: channel/carrier protein, same as conc. gradient

active diffusion: carrier protein, OPPOSITE conc. gradient

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14
Q

what terms are used to refer to levels of tonicity?

A

Equal conc. : isotonic

low conc. : hypotonic

high conc. : hypertonic

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15
Q

what are gated channels and membrane potential, and what are they used for?

A

gated chanels have the ability to open or close in response to certain stimuli, this allows for better control over how much of the molecule traverses the membrane

membrane potential is when a voltage is applied to a channel. This is to allow ions to pass through better

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16
Q

How are transmembrane proteins bound to the membrane?

A

they can be bound to lipid anchors that are directly attached to the tail of a phospholipid

or they can use non polar domains to span the membrane and stay there due to positive interactions between the inside of the membrane

17
Q

What is osmosis?

A

diffusion of water across a membrane, opposite of the concentration gradient (high water to low water)

18
Q

how does the tonicity of the environment affect a cell?

A

isotonic: no effect
hypotonic: the cell swells, less water concentration inside
hypertonic: cell shrivels, more water conc. inside

19
Q

What are hydrostatic and osmotic pressures?

A

hydrostatic pressure is the force of the cytoplasm on the membrane and exerted by the membrane onto the cytoplasm, osmotic pressure is the force of water on the membrane and the membrane applying force to stop water from entering the cell

20
Q

What methods do cells have of regulating osmotic and hydrostatic pressures?

A

extrusion: physically pump out water

isosmotic regulation: regulate concentrations by displacing

Turgor pressure: stores ions in the vacuole, then it absorbs more water. The cell wall resists the pressure

21
Q

What is co-transport?

A

a form of active transport in which more than 1 molecule traverses the membrane against it’s concentraition gradient

22
Q

What is a redox reaction (in biology)?

A

It is the transfer of an electron, this electron is bounded to a proton, making it the transfer of a hydrogen atom. The molecule gaining the H is reduced, the other is oxidised.

23
Q

How do enzymes speed up reactions and stabilize intermediates

A
  • orienting the substrates
  • bringing them closer
  • stressing particualr bonds
24
Q

What is induced fit?

A

When a substrate binds to the active site of an enzyme, the tertiary interactions in the enzyme change, thus the shape of the enzyme changes slightly to grip the substrate

25
What is the difference between a biochemical pathway and a multi enzyme complex?
a biochemical pathway is not necessarily in one place, it can include the use of a multienzyme complex. It describes the chemical reactions rather than the enzyme.
26
what is the advantage brought by multienzyme complexes?
the enzymes are closer, so the substrate will have less far to travel to react with the next enzyme, thus it is more efficient.
27
What affects the rate of enzymatic activity, and why?
concentration of the substrate, more chance to have collisions binding affinity, the higher the bonding affinity the higher the chances are that the substrate will bind to the enzyme when coming into contact temperature, not too low so that the molecules move faster, but not too much to denature the enzymes ph: if too acidic or basic, the presence of too much or too few H+ or OH- ions will alter the enzyme and not allow it to function
28
What is Km?
the concentration of substrate required to have half the max reaction speed
29
what is competitive and non-competitive inhibition?
It is when an inhibitor binds to the enzyme. Comp: binds to the active site, reacts instead. will leave and the substrate will go after. must outcompete, changes Km non-comp: will bond to the allosteric site and change the shape of the enzyme, thus deactivating it. cannot compete, changes Vm
30
what is feedback inhibition and why is it important?
it is when a product of a biochemicla pathway acts as an inhibitor for earlier steps of the pathway. Allows for systems to autoregulate, not produce too much substrate.
31
what is anabolism vs catabolism?
anabolsim is the set of reactions in which the cell builds what it needs. these reactions are endergonic catabolism is the set of reactions that power anabolism by breaking down nutrients for energy
32
What are the 2 methods of making ATP?
substrate level phosphorylation, adding phosphate to ADP oxidative phosphorylation, collecting energy from excited electrons to generate energy to add a phosphate to ADP
33
Where does glycolysis occur?
In the cytoplasm
34
what is the yield of glycolysis per glucose molecule?
2 ATP, 2 Pyruvate, 2 NADH
35
In general terms, what are the steps of glycolysis?
first, the glucose molecule is primed for the reaction, this adds 2 phosphate groups and costs 2 ATP then, cleavage reactions occur, the molecule is cut in two to form 2 G3P. Then, energy is generated by oxidation and substrate level phosphorylation occurs to make ATP