Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

BIO1140 > Lecture 4: The Chemistry Of Life > Flashcards

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

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

A

Matter; matter; elements

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

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

A

Oxygen
Carbon
Hydrogen
Nitrogen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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%

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

The human body is ___% water

A

60-70

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

The chemistry of life centres around which atom?

A

Carbon

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What are the four major categories of macromolecules?

A

Carbohydrates
Lipids
Proteins
Nuclei acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

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

A

Macromolecules

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

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

A

Chemical energy; storage; structural

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Nucleic acids are polymers called …?

A

Polynucleotides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

Each nucleotides is made up of monomers called ..?

A

Nucleotides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

What are 2 types of nuclei acid?

A 
Deoxyribonucleic acid (DNA)
Ribonucleic acid (RNA)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

Must know at least 2-3:

Function of proteins:

A 
Catalysing chemical reactions (enzymes)
Structural support
Storage
Transport
Cellular communications 
Movement 
Defence against foreign substances
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

A _______ is a biologically functional molecule that consists of one or more polypeptides.

A

Protein

29
Q

________ are unbranched polymers composed of _________ monomers.

A

Polypeptides; amino acid

30
Q

Protein Structure and function

A

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
Q

What is key to understand about amino acid monomers?

A

That properties and grouping and relate to function for amino acid monomers

32
Q

What are the types of amino acids?

A

Non-polar (hydrophobic)
Polar (hydrophilic)
Electrically charged amino acids: (hydrophilic): acidic(-) and basic (+)

33
Q

What is a primary structure in proteins?

A

A. Primary structure is the order of amino acids determined by inherited genetic material, where the amino acids are joined by peptide bonds

34
Q

Secondary structure:

Examples of structures:

A

Result from hydrogen bonds between the backbone of peptides.

ex. Alpha-helix (coil), beta-planted sheet (folded structure)

35
Q

Proteins - tertiary structure

A

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
Q

Proteins - Quaternary Structure

A

Occurs when two or more polypeptides chains form a macromolecule

37
Q

What is an example of a quaternary structure?

A

Hemoglobin

38
Q

Sickle-cell disease

A

A change in primary structure: an amino acid substitution in hemoglobin

39
Q

Levels of protein structure

A

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
Q

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

A) On the exterior surface of the protein

41
Q

What isn’t a true bond type but a biologically important type of interaction?

A

Hydrophobic interactions

42
Q

What is the simplest organic molecule?

A

Hydrocarbons

43
Q

Most biomolecules are not ________ because they contain other ________ groups.

A

Hydrocarbon, functional

44
Q

A ______ variety of macromolecules can be built from a ____ set of building blocks.

A

Large;small

45
Q

What are the distinctive properties important to each macromolecule?

A

Their carbon skeleton & their attached functional groups

46
Q

What are the polymers which are life’s macromolecules?

A

Carbohydrates, proteins, and nucleic acid

47
Q

Polymer

A

A long molecule consisting of many similar building blocks

48
Q

Monomers

A

Small, repeating molecules that serve as building blocks

49
Q

What is a protein?

A

A biologically functional molecule that consists of 1+ polypeptides

50
Q

Polypeptides

A

Unbranched polymers composed of amino acid monomers

51
Q

Amino acid

A

Organic molecules with carbonyl and amino groups

52
Q

All proteins are:

A

Polymers constructed from the same set of 20 amino acids

53
Q

Amino acids differ in their properties because of:

A

Differing R groups (side chains)

54
Q

What makes an amino acid basic?

A

A positively charged side chain

55
Q

What makes an amino acid acidic?

A

A negatively charged side chain

56
Q

How can you identify if a molecule is polar or non polar?

A

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
Q

What makes an amino acid hydrophobic /hydrophilic?

A

Hydrophobic: nonpolar
Hydrophilic: polar and electrically charged side chains

58
Q

Peptide bonds

A

The glue between amino acids

59
Q

What are the reinforces in tertiary structures?

A

Strong covalent bonds called désulfite bridges reinforce protein’s structure

60
Q

Disulfide bridges

A

Strong covalent bonds that reinforce protein’s structure

61
Q

A change in primary structure can affect:

A

A protein’s structure and function

62
Q

What will affect a protein’s structure and function?

A

A change in its primary structure

63
Q

Protein folding relates to:

A

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
Q

What determines protein structure?

A 
Primary structure 
Physical conditions
Chemical conditions
Change in pH
Change in salt concentrations 
Change in temperature 
Change in environmental factors
65
Q

Conditions that affect a protein cause it to:

A

Denature/unravel

66
Q

Denatured proteins are biologically ______

A

Inactive

67
Q

What are ex of improperly folded proteins?

A

Alzheimer’s and mad cow disease

68
Q

What is an example of irreversible dénaturation

A

Cooking an egg, albumin egg protein changes state

69
Q

Process from and to normal protein/denatured protein

A

Denaturation and renaturation

BIO1140 (5 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions