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Biology > B1 form and function of molecules > Flashcards

B1 form and function of molecules Flashcards

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1
Q

Polymer

definition

A

a chain of repearting monomers

umbrellar term for polysaccharides and polypeptides

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2
Q

monomer

definition

A

the building blocks of macromolecules

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3
Q

polysaccharide

definition

A

many monosaccharides chemically bonded together for energy storage

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4
Q

monosaccharide

definition

A

one sugar units that are the monomers of carbohydrates

can be pentose or hexose

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5
Q

polypeptide

definition

A

a series of amino acids chemically bonded together

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6
Q

condensation reaction

explain

A

joins monosaccharides together to form polysaccharides by removing the H from one and the OH from another to form a waste product of water

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7
Q

Monosaccharides (glucose) are the monomers of…….

A

carbohydrates

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8
Q

fatty acids and glycorol/phosphates are the monomers of……

A

lipids

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9
Q

amino acids are the monomers of……

A

proteins

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10
Q

nucleotides are the monomers of……..

A

nucleic acids

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11
Q

properties of glucose

4 total

A

contains 5 polar OH groups therefore the whole molecule is polar
1. molecular stability
(due to covalent bonds)
2. high solubility in water
(due to polarity)
3. easily transported
(due to solubility)
4. yields high energy when oxidised
(breaks high energy covalent bonds)

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12
Q

what are the 4 macromolecules

A

carbohydrates
lipids
proteins
nucleic acids

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13
Q

hydrolysis

explain

A

turns polymers into monomers by using water to add a H to one monomer and OH to another monomer breaking the bond and both monomers have another hydroxyl group

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14
Q

Amino acids contain

structure

A
  1. central carbon
  2. amine group (NH2)
  3. carboxyl group (COOH)
  4. unique R group
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15
Q

Condensation of amino acids into (dipeptides/proteins)

A

the H from the amine group of one amino acid is remove and the OH from the carboxyl group of another to from a peptide bond and water

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16
Q

peptide bond

explain

A

the strong covalent bond that forms when two amino acids bond together

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17
Q

Elements in Carbohydrates

A

Carbon, hydrogen, oxygen (1:2:1)

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18
Q

Elements in lipids

A

Long carbon hydrogen chains and a small amount of oxygen

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19
Q

Elements in proteins

A

Carbon, Hydrogen, oxygen and nitrogen

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20
Q

Starch (amylose and amelopectin) are examples of…….

A

carbohydrates

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21
Q

glycogen is an example of……

A

a carbohydrate

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22
Q

cellulose is an example of……

A

a carbohydrate

23
Q

Saturated fatty acids contain…..

A

single carbon to carbon bonds

24
Q

properties of saturated fatty acids

A
  • densly packed
  • high melting point so solid at room temp
25
Q

monounsaturated fatty acids contain……

A

one double carbon to carbon bond, the rest are single

26
Q

polyunsaturated fatty acids contain….

A

more than one double carbon to carbon bond

27
Q

properties of monounsaturated fats

A
  • less dense
  • low melting point so liquid at room temp
28
Q

what makes up a triglyceride

A

a glycerol backbone and three fatty acid tails joined by esther linkages (condensation reaction)

29
Q

triglycerides are examples of……

A

lipids

30
Q

properties of triglycerides

A
  • non-polar
  • hydrophobic
  • stable energy storage
  • contain lots of energy
  • poor heat conductors so good insulation
31
Q

phospholipids are an example of…..

A

lipids

32
Q

properties of phospholipids

A
  • contain 1 glycerol, 2 fatty acids and 1 phosphate group
  • amphipathic (non-polar and polar regions)
33
Q

steroids are an example of…..

A

lipids

34
Q

properties of steroids

A
  • made of 4 fused carbon hydrogen rings
35
Q

how many amino acids are there

A

20 unique 9 are essential

36
Q

amino acids contain….

A

an amine group, an R group and a carboxyl group

37
Q

R groups can be…..

A

polar, non-polar and charged

38
Q

what bonds to amino acids form firectly between eachother

A

peptide bonds

39
Q

collagen is an example of…..

A

a protein

40
Q

properties of collagen

A
  • 3 polypeptide chains
  • fibrous
  • used for tendons and ligaments
41
Q

insulin is an example of…..

A

a protein

42
Q

properties of insulin

A
  • globular
  • non-conjugated
  • 2 polupeptide chains attached by disulfide bridges
43
Q

haemoglobin is an example of…..

A

a protein

44
Q

properties of haemoglobin

A
  • globular
  • conjugated
  • 4 polypeptides (2 alpha globin, 2 beta globin)
  • 4 heme groups
45
Q

What is the primary structure of a protein

A

the specific sequence of amino acids held together by strong peptide bonds

determined by DNA sequences

46
Q

what can alter primary structure?

A

mutation

47
Q

what is the secondary structure of a protein?

A

hydrigen bonds between the c and o, and n and h of two amino acids as they are charged

48
Q

what alters secondary structure

A

bonds break in extreme environments

49
Q

what is the tertiary structure of a protein?

A

the unique folding created by R group interactions

50
Q

types of r group interactions

A
  1. disulfide bridges between cycstines
  2. ionic bonds
  3. hydrogen bonds
  4. hydrophibic interactions
51
Q

what can break tertiary structure?

A
  1. mutations if they change the r groups
  2. denaturation in extreme temps
52
Q

what is the quaternery structure of a protein?

A

the coming together or many polypeptides (non-conjugated) and non protein parts (conjugated) by r group interactions

changes to shape same as for teriary

53
Q

Anabolic reaction

A

when two or more substrates form one product

e.g. photosynthesis

54
Q

catabolic reaction

A

one substrate breaks down to form two or more products

e.g. digestion

Biology (12 decks)

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