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Physiology > Biomolecules (Topic 1) > Flashcards

Biomolecules (Topic 1) Flashcards

1
Q

What do atoms share? (2)

A

Electrons

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2
Q

What are the strongest bond types? (2)

A

Nonpolar and polar

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3
Q

What are nonpolar characteristics? (2)

A
  • They share electrons equally
  • no partial charges
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4
Q

What are polar characteristics? (2)

A
  • unequal electron sharing
  • has partial charges
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5
Q

What is a solute? (4)

A

substance dissolved in a liquid

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6
Q

What is the solvent? (4)

A

The liquid in which solutes dissolve

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7
Q

What is a solution? (4)

A

solutes dissolved in a solvent

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8
Q

What does it mean to be hydrophilic? (4)

A
  • Water loving
  • polar and/or charged things
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9
Q

What does it mean to be hydrophobic? (4)

A
  • water fearing
  • nonpolar and/or not charged things
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10
Q

What does it mean to be amphipathic (amphiphilic)? (4)

A
  • to have hydrophilic and hydrophobic ends
    (not both on the same end)
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11
Q

What is pH? (5)

A

The amount of H+ in a solution
(pH = -log[H+])

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12
Q

Hydrogen ion is the same as what? (5)

A

proton

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13
Q

As proton concentration increases, what happens to pH? (5)

A

pH decreases and proton concentration increases and vice versa

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14
Q

What is a buffer? (5)

A

Something resistant to pH change

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15
Q

What is the primary buffer system?
What does its direction depend on? (5)

A

H2CO3 <–> H+ + HCO3-
- Its direction depends on pH. if pH is low, the system moves to the left

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16
Q

Why are they called carbohydrates? (6)

A

Because they are made of hydrocarbons (Cs and Hs)

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17
Q

What are the functions of carbohydrates? (6)

A
  • energy structure
  • storage
  • cell signaling
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18
Q

What are the different sizes of carbohydrates? (6)

A
  • monosaccharides
  • disaccharides
  • oligosaccharides
  • polysaccharides
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19
Q

What are monosaccharides?(6)

A
  • “one” saccharide
  • examples: glucose, fructose, galactose
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20
Q

What are disaccharides? (6)

A
  • Two simple sugars linked by a dehydration reaction
  • ex: sucrose, lactose, maltose
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21
Q

What are oligosaccharides? (6)

A
  • “few” (no distinct number) between di and poly.
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22
Q

What are polysaccharides? (6)

A
  • “many” polymers of glucose
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23
Q

What are plant polysaccharides? (6)

A

Starches and cellulose

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24
Q

What are animal polysaccharides? (6)

A

glycogen

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25
Q

What has more calories starch or cellulose? (7)

A

Starch

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26
Q

What is the difference between starch and cellulose? (7)

A
  • they have different orientations
  • there are enzymes to break down starches but not cellulose
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27
Q

What is cellulose also known as? (7)

A

fiber

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28
Q

What does glycogen do and where is it found? (8)

A
  • Glycogen exists in the body as a reservoir of available energy
  • found in the liver, kidneys, and muscles
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29
Q

What does the hydrolysis of glycogen do? (8)

A

hydrolysis (breakdown by water) of glycogen from the liver and kidney, leads to release of the glucose monomers into the blood

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30
Q

What is glucose often called? Why? (8)

A
  • blood sugar
  • It is the major monosaccharide found in the blood.
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31
Q

What is a lipid? (9)

A

primarily hydrocarbons (sometimes O)

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32
Q

Are lipids polar or nonpolar? Why? (9)

A
  • nonpolar
  • they are made of C-H bonds (nonpolar covalent bonds)
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33
Q

What are the four subclasses of lipids? (9)

A
  • fatty acids
  • triglycerides
  • phospholipids
  • steroids
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34
Q

What are some functions of lipids? (9)

A
  • energy storage
  • insulation
  • cell membranes
  • hormones (communication)
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35
Q

What are the functions of fatty acids? (10)

A
  • Provide energy for metabolism
  • Regulate cell function
  • Component of triglyceride & phospholipid
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36
Q

Why are they called fatty acids? (10)

A

Because of their carboxylic acid group

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37
Q

Why are they called saturated acids? (10)

A

because there is no room (full of H+)

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38
Q

Why are they called unsaturated fatty acids? (10)

A

Because there is room for more groups/atoms

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39
Q

What are the differences in bonds between saturated and unsaturated fatty acids? (10)

A
  • saturated has all single bonds
  • unsaturated has double bonds where they bend
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40
Q

What are triglycerides? (10)

A
  • the majority of lipids in the body
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41
Q

What are triglycerides often known as? (10)

A

fat

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42
Q

What do triglycerides do? (10)

A

provide energy to cells

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43
Q

What do triglycerides consist of? (10)

A

glycerol (3C alcohol) + three fatty acids

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44
Q

Where do you find phospholipids? (11)

A

In the cell membrane

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45
Q

Are phospholipids polar or nonpolar? (11)

A

They are amphipathic (polar heads and nonpolar tails)

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46
Q

Compare and contrast triglycerides and phospholipids (11)

A

Similarities:
- both have glycerol (3C alcohol)
- both have fatty acids
Differences:
- phospholipids have phosphate groups and their attachments
- phospholipids have 2 fatty acids and triglycerides have three

47
Q

What is different about steroids’ structure than other lipids? (11)

A

They have ring structures

48
Q

What are examples of steroid? (11)

A
  • cholesterol
  • estrogen
  • testosterone
49
Q

What do steroids do? (11)

A
  • depends on the steroid
  • cholesterol regulates membrane fluidity and is the starting point of many hormones
50
Q

If you put a few phospholipids in water how would they orient? (12)

A
  • they would for a micelle
  • tails attract to each other b/c they are hydrophobic (nonpolar)
51
Q

If you put thousands of phospholipids in water how would they orient? (12)

A
  • They would form a bilayer
  • They have hydrophilic (polar) heads so they would face the outside toward the water
  • can’t make a micelle b/c they can only be so big
52
Q

What molecules are nucleic acids? (13)

A
  • DNA
  • RNA
  • ATP
  • GTP
53
Q

What is the function of a nucleic acid? (13)

A
  • info. storage (DNA and RNA)
  • energy transfer (ATP and GTP)
54
Q

What is the monomer of a nucleic acid? (13)

A

A nucleotide

55
Q

What is the difference between deoxyribose and ribose? (13)

A

Deoxyribose is missing an oxygen
- ex: H vs OH

56
Q

What do proteins do? (14)

A
  • storage
  • transport
  • enzymes
  • protection
  • hormones
  • contractile
  • receptors
  • structure
57
Q

How are proteins made? (15)

A

DNA -> RNA -> protein

58
Q

Where are proteins made? (15)

A

The rough endoplasmic reticulum

59
Q

What are the steps for transcription? (15)

A
  • RNA polymerase unzips DNA
  • RNA is made from base pairing (A->U, G->C, T->A, C->G)
  • mRNA detaches from DNA and exits nucleus
60
Q

What are the steps for translation? (15)

A
  • mRNA goes to a ribosome (made of rRNA and proteins) in the cytoplasm or ER
  • codons are read by tRNAs anticodon and form peptide bonds -> peptide chains (proteins) till a stop codon is read
61
Q

What does SRP stand for? (15)

A

signal recognition particle

62
Q

Do all proteins in the rough ER start with a signal peptide? (15)

A

Yes, the signal peptide is what directs them to go to the rough ER in the first place

63
Q

Where are proteins released after being made in the ER? (15)

A

either into the lumen or the membrane

64
Q

If peptides work in the cytoplasm, are the ribosomes free or docked? In the membrane or lumen of ER? (16)

A
  • free
  • N/A
65
Q

If peptides work embedded in the cell membrane, are the ribosomes free or docked? In the membrane or lumen of ER? (16)

A
  • docked
  • membrane
66
Q

If peptides work released from the cell, are the ribosomes free or docked? In the membrane or lumen of ER? (16)

A
  • docked
  • lumen
67
Q

Where do proteins start and end after exocytosis? (16)

A

They start inside the cell and end outside of the cell

68
Q

What are the monomers of proteins? (17)

A

Amino acids

69
Q

What is the basic structure of a protein?
What is the one group that changes? (17)

A

H H O
N C C
H R OH

  • The R group changes depending on the protein
70
Q

What are the different groups of proteins? (17)

A
  • nonpolar (all CHs)
  • polar (not all CHs)
  • Ionized/charged
71
Q

What is a primary structure? (18)

A

A sequence of amino acids

72
Q

How do you get a secondary, tertiary, and quaternary structure? (19)

A

Fold a primary structure

73
Q

What is a peptide? (20)

A

A chain of amino acids

74
Q

What causes peptide folding? (20)

A

Certain interactions that depend on the R-group
- hydrogen bond = polar R
- ionic bond = charged R
- hydrophobic interactions - nonpolar R

75
Q

What is a ligand? (21)

A

any molecule or ion that is bound to a protein

76
Q

How does ligands bind? (21)

A

charged or other interactions

77
Q

What is a binding site? (21)

A

the region of a protein to which a ligand binds

78
Q

True or false
Proteins can have only one binding site (21)

A

False

79
Q

What are the properties of binding sites? (22)

A
  • specificity
  • affinity
  • saturation
80
Q

What is needed for ligands to bind? (23)

A

They must complement in
- shape
- interaction

81
Q

True or false
Some sites only bind one ligand while others can bind many ligands 923)

A

true

82
Q

Which protein is more specific? One that binds to many or only one? (23)

A

Only one

83
Q

What is affinity? (24)

A

The strength of a ligand-protein bond

84
Q

What does the affinity of a binding site determine? (24)

A

How likely it is that a bound ligand will leave the protein surface and return to its unbound state.

85
Q

What binding site has the highest affinity?(24)

A

One that has the same shape and opposite charge

86
Q

What is saturation? (25)

A

fraction or percent of total binding sites that are bound at a given time

87
Q

What does the percent saturation of a binding site depends upon? (25)

A
  • the concentration of unbound ligand
  • the affinity of the binding site for the ligand
88
Q

As ligand concentration increases, what happens to saturation? (25)

A

Saturation increases as ligand concentration increases till saturation reaches 100% then plateaus

89
Q

When does competition occur? (25)

A
  • Between multiple ligands (for the same protein)
  • Multiple proteins (for the same ligand)
90
Q

What are two ways of controlling protein activity? (27)

A
  1. Regulating the number of particular proteins in the cell
  2. Changing protein shape which alters ligand bonding
91
Q

How are the number of particular proteins in a cell regulated? (27)

A
  • protein synthesis/degradation
  • membrane -> up and down regulation (exo and endocytosis)
92
Q

What process brings proteins into a membrane?

A

Exocystosis

93
Q

What are two types of modulation? (27)

A

Allosteric and covalent

94
Q

How many binding sites in allosteric modulation? (28)

A

Protein has two binding sites

95
Q

What happens in allosteric modulation? (28)

A

a modulator binds to a regularity site and changes the shape of the functional site

96
Q

Allosteric activation vs inhibition (28)

A

active- no modulator
Inactive- has a modulator

97
Q

What is covalent modulation? (29)

A

When charged chemical groups bond covalently to some of the protein’s side chains.

98
Q

What is the effect of covalent modulation? (29)

A

Changes shape of functional site

99
Q

What is the most common type of covalent modulation? (29)

A

phosphorylation

100
Q

What does covalent modulation require? (29)

A

Enzymes
- kinase (If ATP is involved)
- phosphatase (if ATP is not involved)

101
Q

How do modulators bind in allosteric modulation? (28)

A

specific interactions with r groups in the binding sites

102
Q

Catabolism (catabolic reactions) (30)

A

the breakdown of molecules (releases energy)

103
Q

Metabolism (30)

A

the body’s chemical reactions

104
Q

Anabolism (anabolic reactions) (30)

A

synthesis of molecules (requires energy)

105
Q

What is a chemical reaction? (30)

A

The breaking and formation of chemical bonds

106
Q

What is an enzyme? How do they work? (31)

A
  • a protein catalyst
  • lowers activation energy and makes it more likely to happen)
107
Q

How many enzymes are in a typical cell? (31)

A

About 4000

108
Q

What three major factors regulate enzyme-mediated reactions? (32)

A
  • Substrate concentration
  • enzyme concentration
  • enzyme activity
109
Q

What is a substrate?

A

the reactant in an enzyme mediated reaction

110
Q

How does substrate concentration affect reaction rate? (32)

A

As substrate conc. increases, reaction rate increases
- eventually plateaus at saturation

111
Q

How does enzyme concentration affect reaction rate? (32)

A

an increase in enzyme conc., increases reaction rate
- plateaus at saturation, but could plateau at a higher reaction rate if there is more enzymes

112
Q

How does enzyme activity (affinity) affect reaction rate? (32)

A

As enzyme affinity increases, reaction rate increases
- if there is a higher affinity, saturation is reached sooner and then plateaus

113
Q

What is a metabolic pathway?

A

a sequence of enzyme-mediated reactions

114
Q

What is feedback inhibition?

A

When an end product of a metabolic pathway inhibits an enzyme early in the pathway

Physiology (15 decks)

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