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Principles > Biochemistry > Flashcards

Biochemistry Flashcards

1
Q

Covalent bond

A

share electron pairs

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2
Q

Ionic bond

A

attraction of opposite forces

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3
Q

Hydrogen bond

A

sharing of an H atom

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4
Q

Hydrophobic interactions

A

interaction of hydrophobic substances in the presence of polar substances (e.g. water)

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5
Q

Van der waals interactions

A

interaction of electrons of non polar substances

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6
Q

Electronegativity

A

attractive force than at atomic nuclei experts on electrons

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7
Q

Phosphorylation

A

addition of a phosphate group, P04(3-) –> this can switch an enzyme on or off

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8
Q

Acylation

A

addition of acyl group COR

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9
Q

Esterification

A

conversion of carboxylic acid to esters in the presence of alcohol

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10
Q

OIL RIG

A

oxidation is loss of electrons

reduction is gain of electrons

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11
Q

What are the oxidation states of carbon

A 
alkane (in fats)
alcohol (in carbohydrates)
aldehyde
carboxylic acid
carbon dioxide
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12
Q

what is the final product of catabolism

A

carbon dioxide

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13
Q

Peptides and proteins consist of

A

amino acids

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14
Q

What is a peptide

A

a ‘sort of unit’ derived either from a protein after cleavage or in a lab

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15
Q

What is a protein

A

a complete unit, encoded in its entirety as one or several peptides

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16
Q

triglycerides, phospholipids and steroids are all members of what group

A

lipids

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17
Q

What is meant by nutrients

A

carbohydrates (sugar)
lipids (fats/oils)
proteins (amino acids)

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18
Q

What is meant by nutrients

A

carbohydrates
lipids
proteins

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19
Q

Lactose

A

galactose-beta-1-4-glucose

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20
Q

Sucrose

A

fructose-alpha-1-2-glucose

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21
Q

Maltose

A

glucose-alpha-1-4-glucose

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22
Q

Cellobiose

A

glucose-beta-1-4-glucose

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23
Q

What is the name for the high energy bonds in ATP

A

anhydride bonds

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24
Q

How is the strain relieved in ATP

A

by removing phosphate groups

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25
Q

Give an example of how ATP is regenerated from a different pathway than the 2ADP …

A

creatine phosphate

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26
Q

Glucogenesis

A

making new glucose from non-carbohydrate precursors, such as pyruvate

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27
Q

What makes a reaction a useful control point

A

high delta g - high free energy change

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28
Q

What shape are hydrogen bonds

A

linear

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29
Q

Why are there hydrogen bonds between water molecules

A
  • polar

- bent –> dipole and tetrahedral shape

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30
Q

When are micelles formed

A

when amphipathic molecules are added to water

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31
Q

Sodium palmitate forms what when added to water

A

micelle

32
Q

What type of amino acids are present in the human body

A

L-type amino acids

33
Q

Describe the basic structure of an amino acid

A

alpha carbon attached to:

  • amino acid group (-NH2)
  • carboxyl group (-COOH)
  • hyrogen (-H)
  • side chain (-R)
34
Q

What is the bond of the protein back bone

A

peptide bond

35
Q

Describe the peptide bond

A

formed between the carboxyl group of 1 amino acid to the amino group of another amino acid,

  • partial double bond character
  • planar
  • strong and rigid
36
Q

What direction do amino acids grow?

A

N-terminal residue to the C-terminal residue (amino acids can be added)

37
Q

pH

A

measure of the no. of protons in a sol

38
Q

pKa

A

measure of the acid strength

39
Q

At what value do buffers tend to resits a change of pH on addition of a small amount of acid or base

A

pKa

40
Q

What is a ZWITTERION

A

compound with no overall electrical charge, but contains separate parts of which one is +ve and the other is -ve

41
Q

What compound contains two titratable groups

A

zwitterion

42
Q

Give an example of a protein that acts as a buffer?

A

haemoglobin in the blood

43
Q

What is meant by the primary structure of a protein

A

the sequence of amino acids

44
Q

What is meant by the secondary structure of a protein

A

the shape/structure of the polypeptide back bone

45
Q

What is meant by the tertiary structure of proteins

A

the 3D structure of the entire polypeptide, including all its side chains

46
Q

What is meant by the quaternary structure

A

the spatial arrangement of polypeptide chains in a protein with multiple subunits

47
Q

What are the three types of secondary structures

A

Alpha helix
Beta sheets and strands
Triple helix

48
Q

Polypeptides can rotate around the angles between

A
  • the alpha carbon and the amino group

- the alpha carbon and the carboxyl group

49
Q

What bond characterises the secondary structure of proteins

A

hydrogen bond

50
Q

Characters of alpha helix

A
  • rod-like
  • one polypeptide chain
  • hydrogen bonds between -C-O and -N-H groups of one amino acid with another 4 residues away
51
Q

What breaks alpha helixes

A

proline

52
Q

Characteristics of beta sheets I

A
  • extended backbone
  • 1+ polypeptide chains
  • parallel or anti-parallel
  • turns between strands
53
Q

Beta pleated sheets

A

-repeated zigzag structures

54
Q

Example of a protein containing both alpha helixes and protein sheets

A

phosphoglycerate kinase

55
Q

Characteristics of collagen triple helix

A
  • water-insoluble fibres
  • right-handed superhelix
  • repeating sequence of X-Y-Gly
  • inter-chain H-bonds
  • covalent inter- and intra- molecular bonds
56
Q

What is the component of bone and connective tissue as well as being the most abundant protein in verterates

A

collagen triple helix

57
Q

What is the repeating sequence of the collagen triple helix?

A

X-Y-Gly
X-amino acid
Y-proline/hydroxyproline
also contains hydroxylysine

58
Q

Bleeding gums are a result of

A

weakened collagen

59
Q

Covent cross linking increases with

A

age

meat from older animals is tougher

60
Q

Ascorbic acid

A

vitamin C

61
Q

Scurvy : bleeding gums, skin discolouration

A 
dietary deficiency of vitamin C
Vitamin C (ascorbic acid) is the enzyme which hydroxylates proline --> hydroxyproline
deficiency of vitamin c results in a reduction of hydroxyproline
WEAKENED COLLAGEN
62
Q

Fibrous proteins and globular proteins are examples of

A

tertiary structures

63
Q

Characteristics of fibrous proteins

A
  • polypeptide chains organised approximately parallel along a single axis
  • consist of long fibres or large sheets
  • mechanically strong
  • insoluble in water and dilute salt solutions
  • play an important structural role in nature
64
Q

Examples of fibrous proteins

A
  • keratin of hair and wool

- collagen of connective tissue of animals including cartilage bones, teeth, skin, and blood vessels

65
Q

Characteristics of globular protein

A
  • proteins which are folded to a more or less spherical shape
  • soluble in water and salt solutions
  • polar side chains on the outside –> hydrogen bonding and ion-dipole interactions
  • substantial sections of alpha-helix and beta-sheet
66
Q

Examples of globular proteins

A
  • myoglobin

- haemoglobin

67
Q

Forces stabilising tertiary structures

A
  • covalent disulphide bonds
  • electrostatic interactions = salt bridges
  • hydrophobic interactions
  • hydrogen bonds (backbone, side chain)
  • complex formation with metal ions
68
Q

Sickle cell anaemia

A
  • single nucleotide sequence change in coding region of the B-chain of haemoglobin A
  • results in altered protein,valine instead of glutamic acid
  • under low 02 conditions, haemoglobin polymerises, results in rigid, sickle shaped cells
  • can block blood flow in capillaries
69
Q

Examples of when proteins spontaneously fold incorectly

A

Alzheimers
Parkinsons
CJD

70
Q

Specialised proteins which aid in the folding of proteins

A

chaperones

71
Q

Mad cow disease

A

caused by infection

72
Q

Creutzfeldt-Jacob disease

A

caused by spontaneous or inherited mutation

73
Q

Detergents, urea, guanidine hydrochlorine all act to denature proteins by

A

disrupting hydrophobic interactions

74
Q

Thiol agents, reducing agents all act to denature proteins by

A

reducing and thereby disrupting disulphide bonds

75
Q

stores oxygen in muscle

A

myoglobin

76
Q

Haemoglobin

A
  • four subunits
  • two alpha and two beta chains
  • each contains a ham group
  • each subunit can bind one oxygen molecule
77
Q

transports oxygen in blood

A

haemoglobin

Principles (6 decks)

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