Molecules & Fundamentals of Biology Flashcards

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1
Q

What type of bonds do carbohydrates make?

A

Glycosidic bonds
**these are joined by dehydration in disacc. (condensation reaction)

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2
Q

What is the opposite of a dehydration reaction and what is the result?

A

Hydrolysis
Covalent bond is broken by the addition of water

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3
Q

What reaction results in a glycosidic bond?

A

Dehydration (condensation reaction)
Water molecule leaves, covalent bond is formed

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4
Q

What type of bonds do proteins make?

A

Peptide bonds

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5
Q

What type of bonds do lipids make?

A

Ester bonds

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6
Q

What type of bonds do nucleic acids make?

A

Phosphodiester bonds

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7
Q

Atoms making up carbs

A

CH2O (Carbon & 1 water)

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8
Q

Atoms making up proteins

A

CHON

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9
Q

Atoms making up lipids

A

CHO

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10
Q

Atoms making up nucleic acids

A

CHONP

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11
Q

What are Monosaccharides? What are the important ones?

A

One sugar
Ribose: 5C
Fructose: 6C
Glucose: 6C

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12
Q

What is maltose

A

glucose+glucose

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13
Q

Polypeptides

A

Polymer of amino acids
Joined by peptide bonds via dehydration synthesis(same as carbs)
Are broken apart via hydrolysis reactions
Chain has N- (amino) and C- terminus (carboxyl)

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14
Q

Primary Protein Structure

A

Amino acid sequence
- connected through peptide bonds

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15
Q

Secondary Protein Structure

A

Peptide backbone with IMFs - forms alpha helices & beta pleaded sheets

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16
Q

Tertiary Protein Structure

A
  • R-group interactions of side chains into 3D structure
  • R-groups create hydrophobic interactions
    (Disulfide bonds/hydrogen bonds)
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17
Q

Quarternary Structure

A
  • Multiple polypeptide chains, forces same as tertiary
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18
Q

Denaturation of proteins

A
  • Loss of function & higher order structures
  • ONLY PRIMARY structure UNaffected
    Affected by:
  • pH changes
  • Temperature changes (high or low)
  • Salt concentrations
  • Chemicals or radiation
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19
Q

Glycoprotein

A

proteins that contain a carbohydrate group

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20
Q

Metalloproteins

A

proteins that contain a metal ion cofactor

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21
Q

What do catalysts do?

A

Reduce the energy of the transition state
Do not shift a chemical reaction or affect spontaneity
Lowering the activation energy

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22
Q

Competitive inhibition

A

Inhibitors compete for active sites
Adding substrate can overcome this type of inhibition

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23
Q

Noncompetitive Inhibition

A

Non-competitive inhibitor binds to allosteric site modifies active site
*Rate of enzyme action cannot be increased by adding more substrate
*Cannot be overcome by adding more substrate
*Substrate and inhibitor don’t “compete” for active site

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24
Q

allosteric inhibition

A

Enzyme conformation changed by binding of inhibitor/activator to different site than active site

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25
Q

Factors that influence membrane fluidity

A

Temperature
Cholesterol
Degrees of Unsaturation

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26
Q

Metabolism

A

Conversion of food into form of energy our body can use

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27
Q

Metabolic pathways

A

product (end result) of earlier rxn serves as reactant (start) of future reaction

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28
Q

Catabolic

A

Breaks down
Releases energy (creates ATP)
Spontaneous rxns
EXERGONIC

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29
Q

Anabolic

A

Builds larger complexes
Uses energy (uses ATP)
Non-spontaneous rxns

30
Q

What is sucrose?

A

glucose+fructose

31
Q

What is lactose?

A

glucose+galactose

32
Q

Chitin:
Function is?
What kinds of linkages?
Is chitin plants, animals or fungi only?

A

Chitin (fungi ONLY!!!)
- provide structure
- 1,4 beta linkages

33
Q

Glycogen:
Function is?
What kinds of linkages?
Is glycogen plants, animals or fungi only?

A

Glycogen (animals ONLY!!)
- energy storage, stored in liver
- 1,4 and 1,6 alpha linkages

34
Q

Starch:
Function is?
What kinds of linkages?
Is starch plants, animals or fungi only?

A

Starch (plants ONLY!!!)
- energy storage
- 1,4 alpha linkages (amylose)
- amylopectin more branched

35
Q

Cellulose:
Function is?
What kinds of linkages?
Is cellulose plants, animals or fungi only?

A

Cellulose (plants ONLY!!!)
- provide structure to cell walls
- humans can’t digest!!!
- 1,4 beta linkages

36
Q

Lipids Function?

A

WISE P!!!
Waterproof (waxes), Insulate, Steroids, Energy, Protection

37
Q

What is a cofactor?

A

Non-protein compound that assists enzymes in reactions

38
Q

What is a ribozyme?

A

An RNA molecule that can act as an enzyme

39
Q

What are holoenzymes?

A

Enzymes+cofactors
Enzymes that are bound to their cofactors

40
Q

What are apoenzymes?

A

Enzymes that are not bound to their cofactors

41
Q

Competitive Inhibition trend

A

Km increases
Vmax stays the same

42
Q

What is Km?
What is Vmax?

A
  1. Substrate concentration at which the velocity (V) is 50% the max
  2. The maximum reaction velocity (increase temp increases enzyme activity)
43
Q

Non-competitive inhibition trend

A

Km stays the same
Vmax increases

44
Q

N-terminus (amino terminus)

A

The side of polypeptide that ends with the last amino acid’s amino group.

45
Q

C-terminus (carboxyl terminus)

A

The side of polypeptide that ends with the last amino acid’s carboxyl group.

46
Q

How do unsaturated fatty acids pack?

A

CIS: have kinks, do NOT pack tightly
TRANS: no kinks, DO pack tightly

47
Q

How do saturated fatty acids pack?

A

Have no double bonds
Pack tightly

48
Q

What are phospholipids made out of?

A

Glycerol backbone
1 phosphate (polar)
2 fatty acid tails (non-polar)
*they are amphipathetic

49
Q

How does cholesterol affect membrane fluidity?

A

HIGH temps: holds membrane together
LOW temps: keeps membrane fluid

50
Q

How does temperature affect membrane fluidity?

A

↑ temperatures increase fluidity
↓ temperatures decrease fluidity

51
Q

What are low-density lipoproteins (LDLs)

A

Have low protein density Work to deliver cholesterol to peripheral tissues
Called “Bad cholesterol” (vessel blockage)

52
Q

What are High-density lipoproteins (HDLs)

A

High protein density
Take cholesterol away from peripheral tissues
Called “Good cholesterol”
* deliver cholesterol to the liver to make bile (reduces blood lipid levels).

53
Q

Waxes?

A
  • Simple lipids with long fatty acid chains connected to mono hydroxy alcohols
  • Hydrophobic protective coatings.
54
Q

Carotenoids?

A

-Lipid derivatives w/ long carbon chains, conjugated double bonds & 6-membered rings @ each end
- Pigments

55
Q

Sphingolipids?

A

A backbone w/ aliphatic (non-aromatic) amino alcohols

56
Q

Glycolipids?

A
  • Lipids found in the cell membrane
  • Have a carb group attached instead of a phosphate group in phospholipids
  • Amphipathic & contain a polar head and a fatty acid chain.
57
Q

What do nucleoSides contain

A

Nucleosides contain a five-carbon sugar and a nitrogenous base.

58
Q

What do nucleoTides contain

A

Nucleotides contain a five-carbon sugar, a nitrogenous base, and a phosphate group.
Tides/TATE

59
Q

How are phosphodiester bonds created?

A
  • From condensation reaction
  • Releases a water as a by-product.
60
Q

Guanine to cytosine bond amount

A

Triple bond H

61
Q

Adenine to thymine bond amount

A

Double bond H

62
Q

What is miRNA

A

miRNA = microRNA. Small RNA molecules that can silence gene expression by base pairing to complementary sequences in mRNA.

63
Q

What is rRNA

A

ribosomal RNA. It is formed in the nucleolus of the cell and helps ribosomes translate mRNA.

64
Q

What is dsRNA

A

double stranded RNA. Some viruses carry their code as double stranded RNA. Protip- dsRNA must pair its nucleotides, so it must have equal amounts of A/U, and C/G.

65
Q

What is tRNA

A

transfer RNA. Small RNA molecule that participates in protein synthesis.

66
Q

Purines

A

PURe As Gold

67
Q

Pyrimidines

A

TCU

68
Q

Kinase adds or removes phosphate group

A

Adds

69
Q

Phosphatase adds or removes phosphate group

A

Removes

70
Q

Enzyme mechanisms of action include:

A
  • Conformational changes that bring reactive groups closer
  • The presence of acidic or basic groups
  • Induced fit of the enzyme-substrate complex
  • Electrostatic attractions between the enzyme and substrate.