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Biology MCAT > Lecture 1 > Flashcards

Lecture 1 Flashcards

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1
Q

4 macromolecules

A

Protein
Lipids
Carbohydrates
Nuclei acids

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2
Q

Amino acid structure

A

Amine - side chain - acid(-COOH)

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3
Q

Condensation reaction

A

Def

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4
Q

Hydrolysis reaction

A

Def

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5
Q

20 amino acids

A
  • structure of R group
  • polar, non polar, acidic, basic, neutral
  • 1-and 3-letter abbrev.
  • charge at physiological pH
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6
Q

Peptide bonds

A

Def and mechanism

N–>C synthesis

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7
Q

Primary structure of protein

A

What is it

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8
Q

Secondary structures

A

Alpha helix

Beta pleated sheet

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9
Q

Tertiary structure

A

Folding is due to side chain interactions within a polypeptide.
Types of interactions:
Non-covalent-
Covalent-

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10
Q

Quaternary structure

A

Interactions of side chains between different polypeptides

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11
Q

Protein function

A 
Enzymes
Hormones
Receptors
Antibodies
Transporters
Pores
Channels
Signaling
Pumps
Porters
Markers
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12
Q

Monosaccharides

A

Formula:
3 common: glucose, fructose, galactose (6-carbon)
2 more: ribose and deoxyribose (5-carbon)

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13
Q

Disaccharides

A

Formula:

3 common: Maltose, sucrose, lactose (glucose based)

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14
Q

Polysaccharides

A

3 common: glycogen, starch, cellulose

Functions: ENERGY, adhesion, and cell surface markers

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15
Q

Lipids

A

Hydrocarbons
Fatty acid
SATURATED fatty acids can STACK up so are SOLID at room temp
Unsaturated fatty acids have double bonds (mono, poly, etc) which create “kinks” in the chain – liquids at room temperature (healthier)
TRANS fats are TERRIBLE - they partially hydrogenate unsaturated fats to make I can’t believe it’s not butter but the double bond goes from Cis –> TRANS which is bad for us.

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16
Q

4 forms of lipids

A

Triglycerides
Phospholipids
Terpenes
Steroids

17
Q

Triglycerides

A

3 fatty acids attached to a glycerol (3-C sugar alcohol) (dehydration reaction) = ester bond “esterifiction”
Functions:
Eaten this way
Store fats this way
STORED ENERGY! Lots of 2-C units to put into Kreb cycle plus no water around so great to store this lipid

18
Q

Phospholipids

A

Glycerol with 2 fatty acids (tails NP) and a phosphate group (head P) attached
“Amphipathic” (both polar and nonpolar)
Functions:
Lipid bilayer membrane

19
Q

Terpenes

A

Built from multiple isoprene units (at least 2)
Triterpenes = 3 terpenes = 6 isoprenes = “squalene”

Function:
Ear wax
Cholesterol precursor

Vitamin A = has a “terpenoids”-like structure

20
Q

Steroids

A 
3 6-membered ring +1 5-membered ring *know that cholesterol drug has 4 rings*
Functions:
Cell membranes
Bile salts
Steroid precursor
21
Q

Thermodynamics

Gibbs Free Energy

A

dG = dH - TdS
(-) spontaneous aka will occur KE>PE (⬆️🔥)
(+) not spontaneous/unfavorable reaction (KE

22
Q

Reaction coupling

A

Reaction that gives OFF energy “Exergonic” dG (-)
Reaction that requires energy “ENdergonic” dG (+)
“energy goes IN”

You can couple two reactions to make them both go. Ex. ATP ADP + Pi (dG -12) is often paired with other reactions that are NOT spontaneous to help them occur.o

23
Q

Kinetics vs thermodynamics

A

Thermodynamics is spontaneous or not, whether it’s gonna happen or not (surfer example) VS kinetics is how FAST it’s going to happen when it does

24
Q

Kinetics

A

A + B ABCD C + D

ABCD: transition state (TS) high energy, transient
Ea: energy of activation, the amount of energy that is needed in order to produce the TS… If you need a lot of Ea, then it takes LONGER to reach the TS, thus the rate ⬇️

25
Q

Reaction coordinate graph (kinetics)

A

Imagine going up an energy hill, the energy you need to walk up the hill is Ea and the top of the hill (or size) is the TS.
A catalyst will make the hill smaller thus bring the TS to a lower energy level, increasing the rate by ⬇️Ea.

26
Q

Catalyst

A

1) stabilize the TS (makes it easier to reach it)
2) ⬇️ Ea thus increase the rate of the reaction

catalysts DO NOT play a role in thermodynamics!!! Kinetics only!

In the body, we call them “enzymes”.

27
Q

Enzymes

A 
Physiological catalysts
Criteria:
1) must ⬆️ reaction rate
2) must not be used up in the reaction
3) they are specific for a particular reaction
28
Q

Enzyme regulation (on off)

A
  1. Phosphorylation

2. Allosteric regulation

29
Q

Enzyme regulation of biochemical pathways

A

Negative feedback is the most common way to regulate a pathway

Positive feedback is the second most common way to drive a pathway in the forward direction —> “exaggerated response” (ex. Blood clotting/ action potentials/ labor contractions/ breastfeeding) will have an external regulator to make it stop! (Ex AP/ baby/ etc)

30
Q

[V] vs [S] graph

A

3 conditions:
1) S«<»>E (saturated, flattening) Vmax is reached
{Vmax depends on the enzyme and the concentration of the enzyme}
{Km is the substrate required to reach half of Vmax}
If the affinity 😍 of the E for S is ⬆️, then the ⬇️ the Km. You’ll need less S bc E ❤️ S, so it’ll hold on tightly to each S it 👀.

31
Q

Inhibitors

A
  1. Competitive (⬆️ Km)
  2. Non-competitive (⬇️ Vmax)
  3. Uncompetitive (⬇️ Vmax, ⬇️ Km)
  4. Mixed inhibition (⬇️ Vmax)

Always assume reversibility!

32
Q

Competitive inhibitor

A

Looks like [S] or [TS] to bind the active site, but cannot turn it into product, thus a reduced rate of product formation. ⬇ PRODUCT formation.

If you have high enough [S] you will eventually hit the same Vmax, but the substrate will have less affinity due to the inhibitor, thus Km will increase.

Blue ball carnival game example

33
Q

Noncompetitive inhibitor

A

Allosteric inhibitor, so although it’s not binding at the active site, it’s changing the conformation of the active site and thus reducing the binding of S and reducing the Vmax. (New Vmax, new Km which is not back at the level it was… So unchanged basically.)

(The Vmax is always lowered due to the allosteric inhibitor! It reduces the amount of “useable” substrate)

34
Q

Uncompetitive inhibition

A

Binds at the allosteric site of the ES complex, locking them together but not allowing them to form a product. Will ONLY bind when the S is bound to the E. Assume reversibility, so this can be switched off and allow product to form since the ES is already joined.

⬇️ Vmax
⬇️Km (increase S affinity)

35
Q

Mixed inhibitors

A

Can bind to the allosteric site of E or to allosteric site of the ES complex.
⬇️ Vmax

Km can vary depending on what it does to the E when it binds to E. If it binds to:
ES: ⬇️ Km
E (changed conformation): ⬆️ Km (comp. inhibitor)
E (doesn’t change conformation): unchanged, doesn’t affect the S to bind, just turns off the enzyme.

36
Q

Lineweaver-Burk Plot

A

Reciprocal graph, think of it in the reverse way. As you move away from the axis, it’s decreasing.

Biology MCAT (2 decks)

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