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Biology AS Level > 1A Biological Molecules > Flashcards

1A Biological Molecules Flashcards

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1
Q

Proteins

A

Polymers made up of the monomers amino acids.

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2
Q

Structural levels of proteins

A

Primary
Secondary
Tertiary
Quaternary

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3
Q

What is the primary structure determined by?

A

The order of bases in a gene determine the sequencing of amino acids in a polypeptide chain.

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4
Q

Where do the hydrogen bonds in the secondary structure of a protein form?

A

Between the negatively charged C=O of the carboxyl group of one amino acid and the positively charged H of the amino group of another amino acid.

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5
Q

Tertiary structure

A
  1. the further folding of the secondary structure
  2. to form a unique 3D shape
  3. held in place by ionic, hydrogen and disulfide bonds
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6
Q

Where do the bonds in the tertiary structure form?

A

Between the R groups of different amino acids.

Disulfide bonds only occur between two sulfur atoms in the R group (cystein)

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7
Q

Quaternary structure

A

A proteins made up of more than one polypeptide chain.

e.g. Hb

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8
Q

What happens if a protein is denatured?

A

The bonds which hold the tertiary and secondary structure in shape break, and therefore the unique 3D shape is lost.

This 3D shape is critical to a proteins function.

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9
Q

What can cause a protein to denature?

A

• too high temperature
• changes in pH

ionic - changes in pH
hydrogen - heat, acidity

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10
Q

Prosthetic group

A

The molecule incorporated in a conjugated protein

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11
Q

Conjugated protein

A

Protein molecules joined with another molecule called a prosthetic group

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12
Q

Lipoproteins

A

Conjugated proteins with a lipid prosthetic group

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13
Q

Glycoprotein

A

Conjugated proteins with a carbohydrate prosthetic group

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14
Q

Proteases

A

protein-digesting enzymes

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15
Q

Peptide bond

A

The bond formed by condensation reactions between amino acids

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16
Q

Compare the energy storage capabilities of lipids and carbohydrates

A

Lipids (especially triglycerides) can store about 3x as much energy as the same mass of carbohydrates

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17
Q

What type of protein is collagen?

A

Fibrous protein

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18
Q

Where in the human body is collagen found?

A

• skin
• matrix of bones
• tendons

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19
Q

In what body structures is keratin found?

A

Hair
Nails

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20
Q

anion

A

a negative ion

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21
Q

cation

A

a positive ion

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22
Q

ionic bonds

A

bonds formed when atoms give or receive electrons; they result in charged particles called ions

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23
Q

covalent bond

A

bonds formed when atoms share electrons; covalent molecules may be polar if the electrons are not shared equally

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24
Q

dipole

A

the separation of charge in a molecule when the electrons in covalent bonds are not evenly shared

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25
Q

polar molecule

A

a molecule containing a dipole

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26
Q

dissociation

A

splitting of a molecule into smaller molecules, atoms, or ions, especially by a reversible process

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27
Q

hydrogen bonds

A

weak electrostatic intermolecular bonds formed between polar molecules containing at least one hydrogen atom

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28
Q

monomer

A

a small molecule that is a single unit of a larger molecule called a polymer

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29
Q

polymer

A

a long-chain molecule made up of many smaller, repeating monomer units joined together by chemical bonds

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30
Q

macromolecule

A

a very large molecule often formed by polymerisation

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31
Q

monosaccharide

A

a single sugar monomer

32
Q

disaccharide

A

a sugar made up of two monosaccharide units joined by a glycosidic bond, formed in a condensation reaction

33
Q

polysaccaride

A

a polymer consisting of long chains of monosaccharide units joined by glycosidic bonds

34
Q

triose sugar

A

a sugar with 3 carbon atoms

35
Q

pentose sugar

A

a sugar with 5 carbon atoms

36
Q

ribose

A

a pentose sugar that is part of the structure of RNA

37
Q

deoxyribonucleic acid

A

a nucleic acid that is the genetic material in many organisms

37
Q

deoxyribose

A

a pentose sugar that is part of the structure of DNA

38
Q

ribonucleic acid

A

a nucleic acid which is the genetic material in some organisms and is involved in protein synthesis

39
Q

hexose sugar

A

a sugar with 6 carbon atoms

40
Q

isomers

A

molecules that have the same chemical formula, but different molecular structures

41
Q

glycosidic bond

A

a covalent bond formed between two monosaccharide units

42
Q

reducing sugar

A

sugars that react with blue Benedict’s solution and reduce the copper(II) ions to copper(I) ions giving an orangey-red precipitate

43
Q

non-reducing sugar

A

sugars that do not react with Benedict’s solution

44
Q

oligosaccharides

A

molecules with between 3 and 10 monosaccharide units

45
Q

ATP

A

adenosine triphosphate, the molecule that acts as a universal energy supply molecule in all cells

46
Q

amylose

A

a complex carbohydrate containing only alpha glucose monomers joined together by 1,4-glycosidic bonds so the molecules form long unbranched chains

46
Q

end products

A

the final products of a chemical reaction

47
Q

amylopectin

A

a complex carbohydrate made up of alpha glucose monomers joined by 1,4-glycosidic bonds with some 1,6-glycosidic bonds so the molecules branch repeatedly

48
Q

ester bonds

A

bonds formed in a condensation reaction between the carboxyl group (-COOH) of a fatty acid and one of the hydroxyl groups (-OH) of glycerol

49
Q

glycogen

A

a complex carbohydrate with many alpha glucose units joined by 1,4- glycosidic bonds with many 1,6-glycosidic bonds, giving it many side branches

50
Q

saturated fatty acid

A

a fatty acid in which each carbon atom is joined to the one next to it in the hydrocarbon chain by a single covalent bond

50
Q

unsaturated fatty acid

A

a fatty acid in which the carbon atoms in the hydrocarbon chain have one or more double covalent bonds in them

51
Q

monounsaturated fatty acid

A

a fatty acid with only one double covalent bond between carbon atoms in the hydrocarbon chain

52
Q

polyunsaturated fatty acid

A

a fatty acid with two or more double covalent bonds between carbon atoms in the hydrocarbon chain

53
Q

esterification

A

the process by which ester bonds are made

54
Q

dipeptide

A

two amino acids joined by a peptide bond

55
Q

collagen

A

a strong fibrous protein with a triple helix structure

56
Q

denaturation

A

the loss of the 3D shape of a protein (e.g. caused by changes in temperature or pH)

57
Q

describe 2 structural features of insoluble proteins

A
  • long chains of amino acids
  • repeating sequences of amino acids
  • parallel chains held with cross links / by hydrogen bonds
58
Q

Which type of fatty acids has more hydrogen atoms?

A

the more hydrogen atoms a fatty acid has the more saturated it is

59
Q

which fatty acids are bad for health?

A

saturated (single bonds only)

60
Q

describe the structure of collagen

A

• fibrous protein
• composed of three polypeptide chains (triple helix)
• held by hydrogen bonds between the chains
• repeating sequence of glycine (every third amino acid is glycine)

61
Q

describe the structure of collagen

A

• fibrous protein
• composed of three polypeptide chains (triple helix)
• held by hydrogen bonds between the chains
• repeating sequence of glycine (every third amino acid is glycine)

62
Q

three types amino acids found in collagen

A
  • glycine
  • proline
  • hydroxyproline
63
Q

what type of proteins is soluble in water?

A

globular proteins

64
Q

what type of protein is insoluble in water?

A

fibrous proteins

65
Q

what is the most common structural protein found in animals?

A

collagen

66
Q

what type of protein is Hb?

A

globular protein

67
Q

when does water reach its max. density?

A

at 4*C

68
Q

what type of bonds joins monosaccharides?

A

glycosidic bond

69
Q

ester bond

A

bond formed in a condensation reaction between a glycerol molecule and a fatty acid

70
Q

peptide bond

A

bond formed in a condensation reaction between two amino acids to form a dipeptide

71
Q

examples of fibrous proteins

A

collagen
keratin
elastin

72
Q

examples of globular proteins

A

haemoglobin
insulin
lysozyme

Biology AS Level (18 decks)

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