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biology - molecules to cells > Section 2: Chemistry of Life > Flashcards

Section 2: Chemistry of Life Flashcards

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1
Q

What are carbohydrates?

A
  • serve as fuel and building material
    -Include sugars and their polymers
    -Monosaccharides/disaccharides and polysaccharides
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2
Q

What are examples of carbohydrates?

A

Monosaccharides: glucose, galactose, fructose
Disaccharides: sucrose, lactose, maltose
Polysaccharides: starch, cellulose (most abundant compound on earth)

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3
Q

Draw a carbohydrate

A

(This can be glucose w ring structure)

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4
Q

What are defining characteristics of Lipids?

A

-Hydrophobic
-Makes membranes, energy, insulation, messengers
-fatty acids, triglycerides, phospholipids
-There key feature is that they are amphipathic: membrane-forming
DO NOT form polymers

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5
Q

Draw cholesterol

A
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6
Q

What are proteins?

A

polymers of amino acids

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7
Q

What are nucleic acids?

A

-Informational polymers made of nucleotides
-DNA makes RNA
-RNA makes protein
-Nucleotides have 3 parts, base, sugar, phosphate

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8
Q

Draw a DNA chain -

A

Base, Sugar, Phosphate

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9
Q

What is the base pair rule?

A

For DNA: A & T
C & G
For RNA: A & U
C & G

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10
Q

What is DNA?

A

a double helix - found by Rosalind Franklin

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11
Q

What are the four classes for biological macromolecules?

A
  • Carbohydrates
  • Lipids
  • Nucleic acids
  • Proteins
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12
Q

What are the different types of carbohydrates?

A

The simplest are monosaccharides (simple sugars) this includes glucose and fructose
-Hydroxyl groups make them water-soluble (dissolve in water)
-Usually occur as polymers: polysaccharides (starch, cellulose)
- A lot of complexity in their chemistry and functions (chitin: in cell wall of fungi) sulfate and dermatan sulfate

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13
Q

What are hydrocarbons?

A

organic molecules with hydrogen and carbon
- many organic molecules, such as fats have hydrocarbon components
-they can undergo reactions that release a large amount of energy

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14
Q

What do nucleic acids do?

A
  • Store, transmit and help express hereditary information
  • Nucleic acids are made of monomers called nucleotides
  • A gene consists of DNA
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15
Q

What is ATP and what is it used for?

A

it is an important source of energy for cellular processes (it really is energy)
- it is an organic phosphate (adenosine triphosphate)
- consists of an organic molecule called adenosine attached to a string of three phosphate groups

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16
Q

What is COPD also known as Chronic Obstructive Pulmonary Disease

A

The enlargement of the alveoli (tiny air sacs in the lungs) accompanied by the destruction of the cell walls ALSO known as emphysema

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17
Q

What are the functions of proteins?

A
  • Cells building blocks
    -They account for more than 50% of the dry mass of most cells
  • Some proteins speed up chemical reactions
  • Other functions are: defense, storage, transport, cellular communication, movement, and structural support
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18
Q

What is an enzymatic protein?

A

Function: selective acceleration of chemical reactions
Example: digestive enzymes catalyze the hydrolysis of bonds in food molecules

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19
Q

What is a defense protein?

A

Function: protein against disease
Example: Antibodies inactivate and help destroy viruses and bacteria

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20
Q

What is a storage protein?

A

Function: storage of amino acids
Examples: casein the protein of milk is the major source of amino acids for baby mammals

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21
Q

What are transport proteins?

A

Function: transport of substances
Examples: Hemoglobin, the iron-containing protein of vertebrate blood, transports oxygen from the lungs to other parts of the body

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22
Q

What are hormonal proteins?

A

Function: Coordination of an organism’s activities
Example: Insulin, a hormone caused by the pancreas, causes other tissues to take up glucose, regulating blood sugar concentration

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23
Q

What are Receptor proteins?

A

Function: response of cell to chemical stimuli
Example: receptors built into the membrane of a nerve cell detect signaling molecules released by other nerve cells

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24
Q

What are Contractile and motor proteins?

A

Function: movement
Examples: motor proteins are responsible for the undulations (moving slowly up and down) of cilia and flagella. Actin and myosin are responsible for the contraction of muscles

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25
Q

what are structural proteins?

A

Function: support
Examples: Keratin is the protein of hair, horns, feathers and other skin appendages. Collagen and elastin proteins provide fibrous framework in animal connective tissue

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26
Q

What are enzymes?

A

They are proteins that act as catalysts to speed up chemical reactions

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27
Q

What are proteins constructed of?

A

the same set of 20 amino acids (this means that they are more easily identified)

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28
Q

What are polypeptides?

A

unbranched polymers built from amino acids

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29
Q

What is a protein?

A

Biologically functional molecule that consists of one or more polypeptides

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30
Q

What are amino acids?

A

organic molecules with amino and carboxyl groups

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31
Q

Why do amino acids differ in their properties?

A

Because they have differing side-chains, called R groups

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32
Q

Draw the base amino acid:

A

Found in red notebook

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33
Q

What are amino acids monomers?

A

amino acids are organic molecules with amino and carboxyl groups
- amino acids differ in their properties due to their differing side chains called R groups

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34
Q

What are polypeptides?

A

Amino acids are linked by covalent bonds called peptide bonds (so amino acids linked together)
- a peptide bond is a polymer of an amino acid
- Polypeptides range in length, from a few to mora than 1,000 monomers (monomer is a bond between two identical molecules)
- Each polypeptide has a unique linear sequence of amino acids, w a carboxyl and and an amino end

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35
Q

Draw an amino acid monomer:

A

(in red notebook for reference)

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36
Q

Draw a polypeptide:

A
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37
Q

What are the four levels of protein structure?

A
  • Primary structure of a protein is its unique sequence of amino acids
  • Secondary structure is found in most proteins, consists of coils and folds in the polypeptide chain
  • Tertiary structure is determined by interactions among various side-chains
  • Quaternary structure results when a protein consists of multiple polypeptide chains
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38
Q

What does the secondary protein structure look like?

A

it is an alpha helix that is spiraled or it is a beta strand that is pleated

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39
Q

What does the tertiary structure look like?

A

It has the a-helix, b-pleated sheet and transthyretin polypeptide

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40
Q

What does the quaternary protein structure look like?

A

Single polypeptide unit and transthyretin protein

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41
Q

Why are there coils in the secondary structure of protein?

A

There are coils and folds because of the hydrogen bonds, repeating in the polypeptide backbone

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42
Q

How does sickle cell disease affect the protein structure of blood cells?

A

Sickle cell disease affects the primary structure which affects the proteins ability to function,
- Sickle cell disease is an inherited blood disorder that results from a single amino acid substitution in the protein hemoglobin
- abnormal hemoglobin molecules cause the red blood cells to aggregate into chains and to deform into a sickle shape

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43
Q

What determines protein structure?

A

chemical and physical conditions can affect structure
- Alterations to pH, salt concentrations, temperature, or other environmental factors can cause proteins to unravel

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44
Q

What is denaturation?

A

when a proteins native structure is lost

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45
Q

What do Parkinson’s and mad cow disease have in common?

A

They are both associated with misfolded proteins

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46
Q

What is matter in the universe made up of?

A

everything is made up of atoms

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47
Q

What are the parts of an atom and there charge:

A

Atoms have protons (positive charge, neutrons (neutral charge), electrons (negative charge)

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48
Q

What are protons and neutrons measured in?

A

They are measured in daltons

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49
Q

Where are valence electrons placed?

A

They are on the outermost shell

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50
Q

What happens when atoms have incomplete valence shells?

A

They can share or transfer valence electrons with certain atoms

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51
Q

What is a compound?

A

a substance containing two or more elements of a fixed ratio

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52
Q

What is a covalent bond?

A

Sharing of valence electrons by two atoms

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53
Q

What is electronegativity?

A

The more electronegative an atom is the more it pulls shared electrons to it

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54
Q

What is a nonpolar covalent bond?

A

atoms share the electron equally

55
Q

What is a polar covalent bond?

A

one atom is more electronegative and the atoms do not share the electron equally

56
Q

What is key to a molecules function?

A

shape and size determine a molecules function - shape also determines how biological molecules recognize and respond to each other

57
Q

What do chemical reactions do to chemical bonds?

A

They make and break chemical bonds

58
Q

What is thermodynamics the study of?

A

the study of energy transformations, in an open system, energy and matter can be transferred between the system and its surroundings

59
Q

what happens in a closed system in thermodynamics?

A

In a closed system energy will exchange with its surroundings but not matter

60
Q

What is the first law of thermodynamics?

A

the energy of the universe is constant. Energy can be transferred or transformed but it cannot be created or destroyed

61
Q

What is the second law of thermodynamics?

A

During every transfer or transformation, some energy is unusable and is often lost as heat.
- Every energy transfer or transformation increases entropy of the universe
- Entropy is the measure of molecular disorder or randomness

62
Q

What is free energy?

A

a measure of a systems instability, its tendency to change to a more stable state

63
Q

what happens during a spontaneous change?

A

free energy decreases and the stability of a system increases

64
Q

What are catabolic pathways?

A

they release energy by breaking down complex molecules into simpler compounds - such as cellular respiration (breakdown of glucose in the presence of oxygen)

65
Q

What are anabolic pathways?

A

they consume energy to build complex molecules from simpler ones (synthesis of proteins from amino acids)

66
Q

When can free energy work?

A

When temperatures and pressures are uniform, as in a living cell

67
Q

What is an exergonic reaction?

A

proceeds with a net release of free energy and is spontaneous

68
Q

What is an endergonic reaction?

A

absorbs free energy from its surroundings and is non-spontaneous

69
Q

What is a catalyst?

A

a chemical agent that speeds up a reaction without being consumed by the reaction

70
Q

What kind of reaction does ATP generate?

A

ATP is an endergonic reaction

71
Q

Why is ATP endergonic?

A

it is a renewable resource that is regenerated by the addition of phosphate group to (ADP)

72
Q

What is ATP composed of?

A

ribose (a sugar), adenine (nitrogenous base), three phosphate groups

73
Q

How does ATP power cellular work?

A

it couples exergonic reactions with endergonic reactions

74
Q

How is the cellular work powered by ATP?

A

the three types of cellular work are powered by the hydrolysis of ATP (breaking of compound due to water)

75
Q

What does ATP hydrolysis lead to?

A

change in protein shape and binding ability

76
Q

What does an enzyme act on?

A

this is called a substrate

77
Q

What forms an enzyme-substrate complex?

A

When an enzyme binds to its substrate

78
Q

Where does a substrate bind on an enzyme?

A

This is called an active site

79
Q

How can you speed up the reaction if the enzyme is saturated?

A

reaction rate can only be sped up by adding more enzyme

80
Q

What are cofactors?

A

they are nonprotein enzyme helpers, they can be inorganic (such as metal in ionic form) or organic

81
Q

What is an organic cofactor called?

A

this is called a coenzyme and includes vitamins, which are vital for our bodies to function in small quantities. Cofactors will sit in the active site and help the substrate bind correctly

82
Q

What is an inactive enzyme called?

A

an inactive enzyme is called apoenzyme

83
Q

What is a competitive inhibitor?

A

they bind to the active site of an enzyme, and compete with the substrate

84
Q

What is a non-competitive inhibitor?

A

it bind to another part of the enzyme, causing the enzyme to change shape and making the active site less effective

85
Q

What are examples of inhibitors?

A

toxins, poisons, pesticides and antibiotics

86
Q

What is allosteric regulation?

A

it either inhibits or stimulates enzyme activity, this happens when a regulatory molecule binds to a protein at one site and affects the proteins function at another site

87
Q

What is feedback inhibition?

A

when the end product of a metabolic pathway shuts down the pathway, prevents the cell from wasting

88
Q

What is cooperativity in enzymes?

A

a form of allosteric regulation that can amplify enzyme activity - cooperativity is allosteric

89
Q

What is selective permeability?

A

it means to allow some substances to cross more easily than others

90
Q

What are fats constructed from?

A

2 smaller molecules: glycerol and fatty acids

91
Q

What are saturated fatty acids?

A

they have the maximum number of hydrogen atoms possible and no double bonds
- They are solid at room temperature (think of butter)
- Animal fats

92
Q

What are unsaturated fatty acids?

A

They have one or more double bonds
- Liquid at room temperature (think oil, like olive oil)
- Found in fish and plants

93
Q

What is cholesterol?

A
  • it is a type of steroid and characterized by a carbon skeleton and four fused rings
94
Q

What does cholesterol do in the membrane?

A

At warm temperatures cholesterol restrains the movement of phospholipids and at cool temperatures it maintains fluidity by preventing tight packing

95
Q

What are peripheral proteins?

A

They are proteins bound to the surface if the membrane

96
Q

What are integral proteins?

A

They penetrate the hydrophobic core, integral proteins that span the membrane are called transmembrane proteins

97
Q

What determines most of a membranes functions?

A

proteins determine most of a membranes function

98
Q

What do aquaporins do?

A

They facilitate the passage of water molecules

99
Q

What is passive transport?

A

Diffusion is an example of passive transport and it is the tendency for molecules to spread out evenly into the available space
NO energy is expended by the cell in passive transport

100
Q

What is osmosis?

A

diffusion of water across a selectively permeable membrane, water diffuses across the membrane from the region of lower solute to higher solute (to even things out/create homeostasis)

101
Q

What is tonicity?

A

the ability of a surrounding solution to cause a cell to gain or loose water, tonicity depends on its concentration of solutes that cannot cross the membrane

102
Q

What does it mean to be isotonic?

A

The solute concentration is the same inside and outside the cell (nothing moving back and forth to create osmosis)

103
Q

What does it mean to be hypertonic?

A

the solute concentration is greater outside of the cell than inside (loss of water, cell shrivels)

104
Q

What does it mean to be hypotonic?

A

the solute concentration inside the cell is more so it gains water (cell wall burst, water floods in)

105
Q

What is facilitated diffusion?

A

transport proteins speed the passive movements of molecules across the plasma membrane

106
Q

What is a gated channel in facilitated diffusion?

A

ion channels open or close in response to a stimulus and these are considered gated

107
Q

Is facilitated diffusion still considered passive transport?

A

yes, because it moves the solute down the concentration gradient (no energy is required)

108
Q

What is active transport?

A

this requires energy, usually in the form of ATP to move substances against their concentration gradients, proteins involved in active transport are carrier proteins

109
Q

What is the sodium potassium pump?

A

This is a transport protein that is energized by transfer of a phosphate group from the hydrolysis of ATP

110
Q

What is membrane potential?

A

it is the voltage across the membrane, the cytoplasmic side of the membrane in negative in charge relative to the extracellular side

111
Q

What is a electrogenic pump?

A

a transport protein that generates voltage across a membrane (the major example of this is the sodium potassium pump). For plants, fungi and bacteria the main electrogenic pump is a proton pump

112
Q

What is Cotransport?

A

when active transport of a solute indirectly drives the transport of another substance

113
Q

What is exocytosis?

A

In exocytosis transport vesicles migrate to the membrane, fuse with it, and release their contents outside the cell, many secretory cells use exocytosis to export their products (especially cells of the digestive tract)

114
Q

What is endocytosis?

A

When the cell takes in macromolecules by forming vesicles from the plasma membrane (reversal of exocytosis)

115
Q

What is digestion?

A

the process of breaking down food into molecules small enough to absorb (starts in the mouth)

116
Q

Why does the small intestine have a huge surface area?

A

This is because of villi and microvilli

117
Q

Where is excess energy first stored?

A

in the liver and muscle cells in a polymer called glycogen (branched chain form of glucose)

118
Q

How are carbohydrates broken down?

A

They are broken down into glucose by various enzymes, some glucose is used immediately but the majority enters the blood stream triggering insulin release and the uptake of glucose into cells

119
Q

What is Acetyl-CoA?

A

it come from metabolized carbohydrates, fats, and proteins, it is and important part of the process which creates the energy molecule called ATP

120
Q

What is Ghrelin?

A

it is a hormone secreted by the stomach wall, that triggers feelings of hunger before meals

121
Q

What is insulin?

A

it is a hormone from the pancreas secreted in the small intestine after meals

122
Q

What is leptin?

A

produced by adipose (fat) tissue, suppresses appetite and plays a role in regulating body fat levels

123
Q

Where are insulin and glucagon both produced?

A

They are produced in the pancreas

124
Q

What makes glucagon and insulin?

A

Alpha cells make glucagon and beta cells make insulin

125
Q

What triggers the synthesis of glycogen?

A

higher insulin levels triggers the synthesis of glycogen

126
Q

What is glucose useful for?

A

it is useful for short bursts of energy without the use of oxygen (but the breakdown of amino acids and fats requires oxygen)

127
Q

What is glycolysis? and what type of process is it?

A

Glycolysis is the breakdown of glucose by enzymes, releasing energy and pyruvic acid, this is an exergonic process

128
Q

What is glucogenesis and what type of process is it?

A

Glycogenesis is the synthesis of glucose and is an endergonic process

129
Q

What happens to triglycerides in the lumen of the gut?

A

triglycerides aggregate (formed by combining several elements) into fat globules as a consequence of aqueous environments

130
Q

What do bile salts do?

A

break down fat globules so that triglycerides can be accessed

131
Q

What do epithelial cells do?

A

they absorb fatty acids and monoglycerides then recombine them back into triglycerides

132
Q

What happens when the body needs energy?

A

adipose cells mobilize the triglycerides into free fatty acids and glycerol, which are then released into the blood

133
Q

What kind of process is fatty acid breakdown?

A

this is an oxidative process that has 4 steps

134
Q

What is Malonyl-CoA?

A

it is a key inhibitor of fatty acid oxidation and controls the switch between fatty acid synthesis and oxidation

biology - molecules to cells (4 decks)

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