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Foundation to Bioscience 1 > Biological molecules > Flashcards

Biological molecules Flashcards

1
Q

What length unit are macromolecules measured in?

A

Nanometres

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2
Q

What’s the typical size of cells?

A

15-50 micrometres

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3
Q

Why is the cell’s plasma membrane important?

A

It regulates what enters and leaves the cell, thereby maintaining the optimum internal environment

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4
Q

What is the cytosol?

A

The water-soluble components of cell cytoplasm, constituting the fluid portion that remains after removal of the organelles and other intracellular structures.

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5
Q

What are the different types of chemical bonds found in biological molecules?

A
  • Covalent- a very strong intramolecular bond
  • Ionic- a strong intramolecular bond
  • Hydrogen bonds- weak, intermolecular bond
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6
Q

What is the most common physiological solvent?

A

Water, which makes up about 70% of living organisms’ mass

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7
Q

Which 6 elements make up about 99% of all living material?

A

Hydrogen, oxygen, carbon, nitrogen, phosphorus, calcium

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8
Q

What are other key elements (5)?

A

Sodium, magnesium, chlorine, potassium, sulfur.

They make about 0.85% of living materials

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9
Q

Name the four classes of biologically important molecules

A

Proteins
Nucleic acids
Carbohydrates
Lipids

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10
Q

What percentage composition of living tissues are macromolecules?

A

30%

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11
Q

Which class of macromolecule has the highest percentage composition?

A

Proteins (55% of macromolecules in tissues are proteins)

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12
Q

What percentage of macromolecules are nucleic acids?

A

27%

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13
Q

What percentage of macromolecules are carbohydrates?

A

12%

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14
Q

What percentage of macromolecules are lipids?

A

6%

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15
Q

What is the basic unit of polymers?

A

Monomers

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16
Q

How are monomers linked together to form polymers?

A

Through condensation reactions, with the release of a water molecule

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17
Q

How are polymers broken down to form monomers?

A

Through hydrolysis reactions

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18
Q

What is the basic monomer of proteins/polypeptides?

A

Amino acids

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19
Q

What is the basic monomer of nucleic acids?

A

Nucleotides

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20
Q

Why is carbon the basis of biogenic molecules?

A

Carbon can form many different types of molecules- straight chain, branched chain, cross-links, ring structures, double bonds. It’s able to be part of different functional groups as well.

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21
Q

How long ago did the first cells begin to evolve?

A

3 billion years ago

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22
Q

What was needed to start producing organic molecules?

A

Sufficient organic material, energy, an inorganic matrix

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23
Q

Where did life on Earth evolve from?

A

Single-celled organisms in the oceans

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24
Q

What were early protocells made from?

A

Probably made from groups of amino acids

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25
Q

Give a reason for one common ancestor for life on Earth

A

We all share a common genetic code

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26
Q

What are self-catalysing reactions?

A

A reaction where the formation of the final products act to stimulate/catalyse the first reactions

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27
Q

What were the earliest signalling molecules?

A

Amino acid-like molecules

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28
Q

What is a protein?

A

A chemical made up of one or more chains of amino acids.
≥3 AA= polypeptide
> a few hundred AA= a protein

29
Q

What is the bond that links two amino acid residues together?

A

A peptide bond

30
Q

Name the reaction that takes place between amino acids to form a peptide

A

Condensation because a water molecule is released

31
Q

What’s the difference between simple proteins and conjugated proteins?

A

Simple proteins are made up of only amino acids. Conjugated proteins have other groups attached to the amino acid chain.

32
Q

Give the four levels of protein structure

A

Primary
Secondary
Tertiary
Quaternary

33
Q

What is the primary structure of proteins?

A

The chain of amino acids

34
Q

What is the secondary structure of proteins?

A

The local folded structures that form within a polypeptide due to interactions between atoms of the backbone.

35
Q

What is the tertiary structure of proteins?

A

The final 3D conformation of the polypeptide

36
Q

What is the quaternary structure of proteins?

A

The arrangement of subunits in a multi-subunit protein

37
Q

What are the bonds that stabilise the tertiary structure?

A

Ionic bonds, hydrogen bonds, hydrophobic interactions, van der Waals interactions

38
Q

What are some of the names of multimeric proteins?

A

Dimer (2 subunits)
Trimer (3 subunits)
Tetramer (4 subunits)

39
Q

Define denaturation

A

The irreversible destruction of the protein’s 3D shape.

40
Q

Give examples of denaturing agents

A 
Heat 
pH
organic solvents 
urea
detergents
mechanical stress
41
Q

Why does denaturation lead to loss of function?

A

The interactions in the secondary and tertiary structures are disrupted, leading to the protein changing shape. This leads to the loss of function

42
Q

Define the term ‘lipid’

A

Lipids are a group of biological molecules that include fats, oils and some steroids. All lipids are hydrophobic

43
Q

Describe the structure of fatty acids

A

A carboxyl group with a hydrocarbon ‘tail’, which are between 4-36 carbons long

44
Q

Where is the omega end of a fatty acid?

A

The end with the terminal CH3 group

45
Q

What is the difference between saturated and unsaturated hydrocarbon tails?

A

Saturated tails don’t have any C=C bonds, whereas unsaturated tails do.

46
Q

What are essential fatty acids?

A

Polyunsaturated fatty acids that animals can’t synthesise, which must be present in the diet.

47
Q

What are lipids often stored as?

A

Triacylglycerol. They consist of 3 fatty acids, joined to a glycerol backbone by ester bonds

48
Q

Why are triacylglycerols efficient energy reserves?

A

Per gram, they release 6 times as much energy as glycogen carbohydrate

49
Q

Define the term ‘amphipathic’

A

Having both hydrophilic and hydrophobic parts

50
Q

What are glycerophospholipids?

A

Glycerol-based phospholipids

51
Q

Why are glycerophospholipids able to form bilayers?

A

Due to their amphipathic nature. Their hydrophobic tail is on the inside of the bilayer, and the hydrophilic head is on the outside

52
Q

What are the monomers of nucleic acids?

A

Nucleotides

53
Q

Name the three components of nucleotides

A

Nitrogenous base
Pentose sugar
Phosphate group

54
Q

Name the four bases in DNA

A

Adenine, guanine, cytosine, thymine

55
Q

Which two DNA bases are the purines?

A

Adenine and guanine

56
Q

Which two DNA bases are the pyrimidines?

A

Cytosine and thymine

57
Q

How is the sugar-phosphate backbone bonded together?

A

With phosphodiester bonds formed through condensation reactions

58
Q

What base replaces thymine in RNA?

A

Uracil, which is a pyrimidine

59
Q

What type of bonding takes place between bases on complementary strands of DNA?

A

Hydrogen bonding

60
Q

Describe the structure of DNA

A
  • Double helix
  • The strands run antiparallel
  • Helix turns every 10 residues
  • DNA has minor and major grooves, where proteins can bind
61
Q

Exposure to what causes the double helix of DNA to unwind? (4)

A

1) extremes of pH
2) increased temperature
3) alcohol, ketones etc
4) exposure to urea or amides

62
Q

Which bonds are broken when the DNA denatures?

A

The hydrogen bonds between the bases

63
Q

How do complementary single strands of nucleic acid reform double helices?

A

By hybridisation.

Can be DNA:DNA, DNA:RNA, RNA:RNA

64
Q

How is DNA stored when not being copied?

A

It’s tightly packed around histones to form chromatin. This folds to form chromosomes

65
Q

What are the three classes of RNA?

A

Messenger RNA
Transfer RNA
Ribosomal RNA

66
Q

What process are all RNA molecules involved in?

A

Protein synthesis.

67
Q

What are the main differences between nuclear DNA and mitochondrial DNA?

A
  • mtDNA is inherited maternally, rather than from both parents
  • mtDNA is circular, and nuclear DNA has a double helix
  • mtDNA isn’t packed into chromatin, but nuclear DNA is
68
Q

What’s the difference between intron and exon regions of DNA?

A

Exon regions code for proteins, and introns are non-coding regions of DNA

Foundation to Bioscience 1 (8 decks)

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