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Introduction to the molecules of life Flashcards

1
Q

Elements necessary for life

A
  • oxygen - 65%
  • carbon - 18%
  • hydrogen - 9.5%
  • nitrogen - 3.2%
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2
Q

Covalent bonding

A

bonding of non-metals by sharing electrons

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3
Q

ionic bonding

A

electrostatic attraction by oppositely charged ions

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4
Q

hydrogen bonding

A

weak electrostatic bonding due to uneven distribution of electrons in some atoms

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5
Q

polymerization

A

monomers, the single units are polymerised (joined together) to form polymer

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6
Q

What are monosaccharides?

A

Single-monomer carbohydrates

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7
Q

What is the most abundant monosaccharide?

A

Glucose.

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8
Q

What is the function of monosaccharides in the body?

A

They serve as a major energy source and are components of nucleic acids and many lipids.

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9
Q

What are oligosaccharides?

A

Carbohydrates made up of 2 to 20 monomers.

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10
Q

What are disaccharides?

A

A type of oligosaccharide containing 2 monomers.

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11
Q

What is a common example of an oligosaccharide?

A

Sucrose.

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12
Q

What is the function of oligosaccharides?

A

They serve structural and regulatory roles and are associated with proteins and lipids.

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13
Q

What are polysaccharides?

A

Carbohydrates made of more than 20 monomers.

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14
Q

What are some examples of polysaccharides?

A

Starch

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15
Q

What is the function of polysaccharides?

A

They have structural and storage roles in all organisms.

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16
Q

What is the monomer unit of carbohydrates?

A

Monosaccharides (e.g. glucose, fructose)

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17
Q

What is the polymer unit of carbohydrates?

A

Polysaccharides (e.g. starch, glycogen, cellulose)

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18
Q

What is the monomer unit of proteins?

A

Amino acids (e.g. arginine, leucine)

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19
Q

What is the polymer unit of proteins?

A

Polypeptides and proteins (e.g. A and B chains of insulin are polypeptides, insulin is a protein)

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20
Q

What is the monomer unit of nucleic acids?

A

Nucleotides (e.g. adenosine, guanosine)

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21
Q

What is the polymer unit of nucleic acids?

A

Nucleic acids (e.g. DNA and RNA)

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22
Q

What is the source of cellulose?

A

Plant

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23
Q

What type of glucose subunit does cellulose contain?

A

β-glucose

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24
Q

What type of glycosidic bonds are found in cellulose?

A

1-4 bonds

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25
Does cellulose have branches?
No
26
What is the shape of cellulose?
Straight and unbranched
27
What is the source of amylose?
Plant
28
What glucose type does amylose use?
α-glucose
29
What type of bonds are found in amylose?
1-4 bonds
30
Does amylose have branches?
No
31
What is the shape of amylose?
Helical/Coiled
32
What is the source of amylopectin?
Plant
33
What type of glucose is found in amylopectin?
α-glucose
34
What types of bonds are found in amylopectin?
1-4 and 1-6 bonds
35
Does amylopectin have branches?
Yes
36
What is the shape of amylopectin?
Moderately branched
37
What is the source of glycogen?
Animal
38
What glucose subunit is in glycogen?
α-glucose
39
What type of bonds are found in glycogen?
1-4 and 1-6 bonds
40
Does glycogen have branches?
Yes
41
What is the shape of glycogen?
Highly branched
42
Starch
- form of glucose - contains amylose and branched amylopectin - stored as granules in chloroplasts - formed when alpha-glucose molecules are joined chemically to form a polymer
43
Cellulose
- form of glucose - formed when beta glucose molecules are joined to form a polymer - stronger - cross linked to form microfibrils of the cell wall
44
condensation reaction
two molecules combine to form a single molecule. a small molecule usually water is removed during the reaction - covalent bond is formed
45
hydrolysis reaction
chemical reaction in which water is used to break down the bonds of a particular substance
46
Amylose
- polysaccharide - linear chains of glucose
47
amylopectin
- polysaccharide - branched chains of glucose
48
glycogen
- chains are shorter with more branches - stored in liver and muscle cells - more compact than starch - break down to release energy
49
lipids - glycerol
3 carbon alcohol with a hydroxyl group attached to each carbon
50
lipids - fatty acids
carboxyl group attached to a long carbon skeleton
51
saturated fats
Fats with no double bonds that are solid at room temp; found in meat, dairy, butter, etc.; can raise LDL cholesterol.
52
unsaturated fats
Saturated fats are a type of fat with single bonds between carbon atoms. They are typically solid at room temperature and found in animal products and some plant oils.
53
What are the two types of unsaturated fats?
1. Monounsaturated fats: One double bond (e.g., olive oil, avocados, peanuts). 2. Polyunsaturated fats: More than one double bond (e.g., fatty fish, flaxseeds, walnuts).
54
Phospholipids
- when added to water, they form into double- layered structures called bilayers - hydrophobic tails point towards the interior - results in a bilayer arrangement found in cell membranes - existence of cells depends on phospholipids
55
triglycerides
- 3 fatty acids joined to glycerol by an ester linkage - can be saturated or unsaturated - major component of blood - adipose tissue is primarily present in the form of triglycerides - covers internal organs and protects them from physical trauma or shock
56
cholesterol
- type of steroid, in animal cell membranes and a precursor from which other steroids are synthesised - synthesised in the liver - can be obtained from eating animal products - needed for cell membranes, brain, nerve tissues, steroid hormones and vitamin D - high levels of cholesterol in the blood clogs arteries, by forming plaques, and may contribute to cardiovascular disease
57
proteins functions
-structural - main component of body tissues e.g. muscles etc -catalytic - all enzymes are proteins, catalysing many biochemical reactions -signalling - many hormones and receptors are proteins -transport and storage - major element in the transport and storage of certain molecules -defence - all antibodies are proteins
58
amino acids
- same general formula - only difference between each one is the nature of the R group which defines an amino acid
59
Peptide bond
- uses the condensation reaction - the OH¯ from the carboxylic group of the amino acid and H¯ from the second amino acids amine group form covalent peptide bond and release a water molecule - uses hydrolysis reaction to break down the peptide bond
60
primary structure
- sequence of amino acids - determined by inherited genetic info
61
secondary structure
- stabilised by hydrogen bonds between specific local sequence of amino acids of the polypeptide backbone - α helix and the β strands which make up β pleated sheets
62
tertiary structure
- 3 dimensional fold - overall shape of polypeptide is stabilised by interactions between R groups - interactions include hydrogen bonds, ionic bonds, hydrophobic interactions, van der walls interactions - strong covalent bonds called disulphide bridges may reinforce the protein structure
63
quaternary structure
- two or more polypeptide chains forms an interacting complex - collagen is a fibrous protein consisting of 3 polypeptide chains coiled like a rope - haemoglobin is globular protein consisting of 4 polypeptide chains : two alpha and two beta chains
64
Factors affecting protein structure
- pH - Salt conc - temp - other environmental factors - denaturation - biologically inactive
65
globular proteins
- spherical shape caused by tightly folded polypeptide chains - chains are folded - hydrophobic groups are on the inside, hydrophilic groups are on the outside - soluble in water - transport proteins - haemoglobin - enzymes - lipase, DNA - hormones - oestrogen, insulin
66
fibrous proteins
- lose structural strength when denatured - formed from parallel polypeptide chains held together by cross-links - these form long, rope like fibres, with high tensile strength and are generally insoluble in water - collagen - main component in connective tissues - ligaments, tendons, cartilage - keratin - main component of hard structure - hair, nails etc - silk - forms spiders webs, and silkworm cocoons
67
Enzymatic proteins
- selective acceleration of chemical reactions eg digestive enzymes
68
defensive proteins
protection against disease eg antibodies
69
storage proteins
storage of amino acids eg - casein, protein of milk - source of amino acid for baby mammals
70
transport proteins
transport of substances eg haemoglobin

Biology (10 decks)

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