Lecture 4: The Chemistry Of Life Flashcards

1
Q

Why are smaller organisms better than larger organisms.

A

They are able to carry out diffusion faster

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2
Q

Where are are the enzymes responsible for biosynthesis of membrane lipids would be located in what part of the cell?

A

The (smooth) endoplasmic reticulum.

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3
Q

Which of the following best explains a child who is unable to play physical games and is very weak:

A) mutation in their mitochondrial DNA leading to reduced ATP production

B) lysosomal storage disease

C) mutation in an enzyme of the smooth ER preventing the detoxifying of drugs

D) mutation in their nuclear DNA resulting in too much ATP production

A

A

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4
Q

Organisms are composed of _______? ______ is made up of _______?

A

Matter; matter; elements

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5
Q

96% of living matter is made up of 4 elements:

A

Oxygen
Carbon
Hydrogen
Nitrogen

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6
Q

What are the trace elements required for life (and what is their role)? What percentage is found in the body?

A

Iron: needed for transportation of oxygen in hemoglobin
iodine: needed for hormone production in the thyroid
copper: needed for multiple metabolic enzymes
which make up less than 0.01%

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7
Q

Why are weak bonds important?

A

They:

  • reinforce shapes of molecules (to interact with cell surface to fit into cell surface receptor, right shape means chemical will work-do its job (ie. morphine will fit into receptor mimicking natural endorphins)
  • help molecules adhere to each other
  • their reversibility can be an advantage
  • large number of weak chemical bond is significant in strength (large number of weak forces can create a large net of force)
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8
Q

The human body is ___% water

A

60-70

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9
Q

Why is water critically important for life?

A

The water molecule has polar covalent bonds and all its atoms can form hydrogen bonds

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10
Q

The chemical bonds between hydrogen and oxygen within water are ______________ bonds. All 3 atoms in a water molecule can form _______ bonds.

A

Polar covalent; hydrogen

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11
Q

Hydrogen bonds are important in understanding water’s many biological functions including:

A
  • its ability to adopt different states
  • its heat capacity/heat of vaporization
  • its cohesive properties (surface tension)
  • its solvent properties
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12
Q

Why is water the solvent of life?

Water can dissolve more substances than any other ______. The compounds dissolved in water are the _______.

A

Solvent; solute

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13
Q

What happens when NaCl dissolves in water?

A

Spheres of hydration are formed around the ions

The ionic regions (Cl-, and Na+) vhgvgvhvhvhvhgvhgv

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14
Q

hydrophobic interactions

A

The relationship between polar-hydrophilic molecules and nonpolar-hydrophobic, which cause hydrophobic molecules to cluster together to reduce contact with the polar molecules.

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15
Q

The chemistry of life centres around which atom?

A

Carbon

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16
Q

Functional groups are components of _________ involved in ___________.
They typically have one or more ____________.
The ________&___________ of functional groups give these ____________ their unique properties.

A

Organic molecules; chemical reactions; electronegative atoms; number; arrangement ; organic molecules

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17
Q

What are the seven functional groups that are most important in the chemistry of life?

A
Hydroxyl
Carbonyl
Carboxyl
Amino
Sulfhydryl
Phosphate
Methyl
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18
Q

What are the four major categories of macromolecules?

A

Carbohydrates
Lipids
Proteins
Nuclei acids

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19
Q

What are large carbon-based molecules that carry out the function of life, where their structure and function are inseparable?

A

Macromolecules

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20
Q

The Diversity of Macromolecules

A

Each cell has thousands of different macromolecules which vary depending on the cell types, and more between individuals of a species, and more between different species.

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21
Q

Building macromolecules

A

Monomers are joined via a dehydration or polymerization reaction which lengthens polymers or they can be broken down by a hydrolysis reaction

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22
Q

carbohydrates provide the cell with ______ and have many _______&______ roles.

A

Chemical energy; storage; structural

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23
Q

What are examples of polymers of glucose (and their role)?

A

Glycogen- energy storage in animal cells

Cellulose- a component in plant cell walls

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24
Q

Nucleic acids are polymers called …?

A

Polynucleotides

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25
Each nucleotides is made up of monomers called ..?
Nucleotides
26
What are 2 types of nuclei acid?
``` Deoxyribonucleic acid (DNA) Ribonucleic acid (RNA) ```
27
Must know at least 2-3: | Function of proteins:
``` Catalysing chemical reactions (enzymes) Structural support Storage Transport Cellular communications Movement Defence against foreign substances ```
28
A _______ is a biologically functional molecule that consists of one or more polypeptides.
Protein
29
________ are unbranched polymers composed of _________ monomers.
Polypeptides; amino acid
30
Protein Structure and function
proteins have polypeptides that range in length from a few to 1000s of amino acids. Their 3D structure is determined by the sequence of amino acids. The function of a protein is determined by its structure. It functions as an ability to recognize and bind other molecules.
31
What is key to understand about amino acid monomers?
That properties and grouping and relate to function for amino acid monomers
32
What are the types of amino acids?
Non-polar (hydrophobic) Polar (hydrophilic) Electrically charged amino acids: (hydrophilic): acidic(-) and basic (+)
33
What is a primary structure in proteins?
A. Primary structure is the order of amino acids determined by inherited genetic material, where the amino acids are joined by peptide bonds
34
Secondary structure: Examples of structures:
Result from hydrogen bonds between the backbone of peptides. ex. Alpha-helix (coil), beta-planted sheet (folded structure)
35
Proteins - tertiary structure
Tertiary structure is the overall shape of a polypeptide which is determined by the interactions between various R groups, which can be hydrogen bonded, ionic bonded, hydrophobic interactions, and van der Walls interactions. The protein is then reinforced by disulfide bridges (strong covalent bonds).
36
Proteins - Quaternary Structure
Occurs when two or more polypeptides chains form a macromolecule
37
What is an example of a quaternary structure?
Hemoglobin
38
Sickle-cell disease
A change in primary structure: an amino acid substitution in hemoglobin
39
Levels of protein structure
Primary protein structure: order of amino acids in chain Secondary protein structure: H-bonding of peptide backbone causing amino acids to fold into a repeating pattern Tertiary protein structure: 3D folding pattern of a protein due to side chain interactions Quaternary protein structure: protein consisting of 1+ amino acid chain
40
Sickle-cell disease is caused you a mutation in the beta-hemoglobin gene that changes a charged amino acid, glutamic acid, to valine, a hydrophobic amino acid. Wher in the protein would you expect to find glutamic acid? On the exterior surface of the protein
A) On the exterior surface of the protein
41
What isn’t a true bond type but a biologically important type of interaction?
Hydrophobic interactions
42
What is the simplest organic molecule?
Hydrocarbons
43
Most biomolecules are not ________ because they contain other ________ groups.
Hydrocarbon, functional
44
A ______ variety of macromolecules can be built from a ____ set of building blocks.
Large;small
45
What are the distinctive properties important to each macromolecule?
Their carbon skeleton & their attached functional groups
46
What are the polymers which are life’s macromolecules?
Carbohydrates, proteins, and nucleic acid
47
Polymer
A long molecule consisting of many similar building blocks
48
Monomers
Small, repeating molecules that serve as building blocks
49
What is a protein?
A biologically functional molecule that consists of 1+ polypeptides
50
Polypeptides
Unbranched polymers composed of amino acid monomers
51
Amino acid
Organic molecules with carbonyl and amino groups
52
All proteins are:
Polymers constructed from the same set of 20 amino acids
53
Amino acids differ in their properties because of:
Differing R groups (side chains)
54
What makes an amino acid basic?
A positively charged side chain
55
What makes an amino acid acidic?
A negatively charged side chain
56
How can you identify if a molecule is polar or non polar?
Polar if it has double bonded oxygen, -OH, or -SH | Non polar is usually hydrocarbon sometimes neutral -NH, and -S attached to carbons (not any hydrogens)
57
What makes an amino acid hydrophobic /hydrophilic?
Hydrophobic: nonpolar Hydrophilic: polar and electrically charged side chains
58
Peptide bonds
The glue between amino acids
59
What are the reinforces in tertiary structures?
Strong covalent bonds called désulfite bridges reinforce protein’s structure
60
Disulfide bridges
Strong covalent bonds that reinforce protein’s structure
61
A change in primary structure can affect:
A protein’s structure and function
62
What will affect a protein’s structure and function?
A change in its primary structure
63
Protein folding relates to:
Where we can/will find a protein within the cell, because hydrophobic core region will contain nonpolar side chains while polar side chains will be on outside able to form hydrogen bonds to water
64
What determines protein structure?
``` Primary structure Physical conditions Chemical conditions Change in pH Change in salt concentrations Change in temperature Change in environmental factors ```
65
Conditions that affect a protein cause it to:
Denature/unravel
66
Denatured proteins are biologically ______
Inactive
67
What are ex of improperly folded proteins?
Alzheimer’s and mad cow disease
68
What is an example of irreversible dénaturation
Cooking an egg, albumin egg protein changes state
69
Process from and to normal protein/denatured protein
Denaturation and renaturation