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Pharm Y1 > The Patient Semester 1 > Flashcards

The Patient Semester 1 Flashcards

1
Q

Which amino acid has the following side chain?

A

Glycine

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2
Q

Which amino acid has the following side chain?

A

Methionine

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3
Q

Which amino acid has the following side chain? -CH2-CH2-CH2- Forming a cyclic peptide

A

Proline

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4
Q

Which amino acid has the following side chain?

A

Alanine

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5
Q

Which amino acid has the following side chain?

A

Valine

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6
Q

Which amino acid has the following side chain?

A

Isoleucine

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7
Q

Which amino acid has the following side chain?

A

Lysine

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8
Q

Which amino acid has the following side chain?

A

Arginine

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9
Q

Which amino acid has the following side chain?

A

Histidine

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10
Q

Which amino acid has the following side chain?

A

Aspartate/Aspartic Acid

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11
Q

Which amino acid has the following side chain?

A

Glutamate/Glutamic Acid

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12
Q

Which amino acid has the following side chain?

A

Tyrosine

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13
Q

Which amino acid has the following side chain?

A

Phenyl Alanine

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14
Q

Which amino acid has the following side chain?

A

Threonine

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15
Q

Which amino acid has the following side chain?

A

Serine

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16
Q

Which amino acid has the following side chain?

A

Cysteine

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17
Q

Which amino acid has the following side chain?

A

Aspargine

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18
Q

Which amino acid has the following side chain?

A

Glutamine

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19
Q

Which amino acid has the following side chain?

A

Tryptophan

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20
Q

Which amino acid has the following side chain?

A

Leucine

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21
Q

Which amino acid has two chiral centres?

A

Isoleucine

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22
Q

How many amino acids are in a chain before it is considered a protein?

A

50 or more

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23
Q

Approximately how many different proteins does one cell contain?

A

>10,000

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24
Q

What percentage of dry cell weight do proteins account for?

A

>50%

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25
Q

Which of the -L or -R isomers exist naturally in amino acids?

A

Only the -L form

Spelling out CORN in a clockwise direction when the hydrogen is drawn as a forward wedge.

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26
Q

What rotation an occur aroud the alpha-carbon atom and what are the torsion angles known as?

A

Free rotation is possible around the alpha-carbon.

C-N by the phi angle

C-O by the psi angle

Favoured rotations leave the R groups in trans configuration

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27
Q

What kind of reaction joins two alpha-amino acids together?

A

Condensation- removal of water

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28
Q

In which part of the cell do amino acids join together to form a peptide?

A

The ribosomes

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29
Q

In what direction is a polypeptide sequence written?

A

From the N-terminus to the C-terminus

30
Q

How long should a single C-N bond measure?

A

1.49 angstrom

31
Q

How long should a double C=N bond measure?

A

1.27 angstrom

32
Q

What is the actual length of a C-N bond within a peptide? And why?

A

The actual length is 1.32 angstrom.

This is because C-N behaves partially like a double bond due to resonance stabilisation.

33
Q

Why is the peptide bond planar?

A

Due to restricted rotation around the C=O bond.

34
Q

Which two amino acids have non-polar side chains?

A

Methionine

Proline

35
Q

Which three amino acids have basic side chains?

A

Lysine

Arginine

Histidine

36
Q

Which two amino acids have acidic side chains?

A

Aspartate

Glutamate

37
Q

Which three amino acids have aromatic side chains?

A

Tyrosine

Phenylalanine

Tryptophan

38
Q

Which five amino acids have hydrophillic side chains but are neutral?

A

Serine

Threonine

Asparagine

Glutamine

Cysteine

39
Q

Which amino acid can form S-S bonds? And where can they form?

A

Cysteine can form S-S bonds interchain and intrachain, altering the overall protein shape.

40
Q

What are the two most common secondary structures of amino acids?

A

Alpha-helixes

Beta-strands

41
Q

Approximately how long is a hydrogen bond within a protein structure?

A

~2.2-3.5 angstrom

42
Q

What torsion angles give an alpha-helix?

A

phi- 57

psi- 47

43
Q

How many residues are there per turn in an alpha-helix?

A

3.6

44
Q

Which -NH does the -CO of an amino acid form a hydrogen bond with?

A

The -NH of the 4th residue ahead

45
Q

What are the four main features of an alpha-helix?

A

R groups extend on the outside

It twists clockwise

Peptide bonds are planar

Peptide bonds are trans

46
Q

How are polypeptide coils formed?

A

Alpha-helices wind around eachother, they are extremely stable

47
Q

How many amino acids must be present to form a Beta sheet?

A

At least 5

48
Q

What are the three main observations in parallel Beta-sheets?

A

R groups point up and down

Strands are held together by Hydrogen bonding between strands

Both strands run from the N-terminus direction

49
Q

What makes antiparallel B-sheets different to parallel ones?

A

In antiparallel sheets, the strands run in opposite directions

50
Q

How many types of Beta turns are there? And what are they used for within a peptide?

A

There are two types and they are used to change direction

51
Q

What are the two types of turn within a polypeptide and what are their characteristics?

A

Loops- contain hydrophillic residues in stretches

Used to connect alpha-helices and beta-sheets

No regular structure

Found on the surface of proteins

Turns- less than five residues

Better defined than loops

52
Q

What are the three levels of structrure complexity?

A

Motifs- arrangement of two of more secondary structural elements

Domain- many folded motifs giving stable, self contained structure

Subunit- combining many domains

53
Q

What are the features of a disulphide bond?

A

Covalent and occur via oxidation

2.2 angstroms in length

167kJ/mol in strength

54
Q

What is the strength of a hydrogen bond inside protein?

A

2-7kcal/mol in strength

55
Q

What is the formula for Gibbs Free Energy? What does it measure?

A

A negative delta G means that it is stable.

56
Q

What is the strength of the van der Waals forces in each C-H within a hydrocarbon?

A

8.4kJ/mol

57
Q

What is the average strength of a hydrophobic bond within a protein?

A

4kJ/mol

58
Q

What is the main driving force for protein binding/folding in aqueous solution?

A

The increased entropy of water as hydrophobic groups bury inside

59
Q

What is glycolysis?

A

Anaerobic degradatin of glucose to produce ATP and pyruvate, occurs in the cytosol

60
Q

What is the size of a prokaryotic cell?

A

1-5 micrometers in diameter

61
Q

What is the size of a eukaryotic cell?

A

10-100 micrometers in diameter

62
Q

How do ribosomes vary from prokaryotes to eukaryotes?

A

In eukaryotes they are 80S in size

In prokaryotes they are 70S in size

In eukaryotic organelles they are 70S

63
Q

What is the thickeness of a membrane?

A

6-10nm

64
Q

What is the basic structure of a phosphoglyceride?

A
65
Q

What are phosphogylcerides derived from?

A

Glycerol or sphingosine

66
Q

Define monounsaturated.

A

Contain only one double bond

67
Q

How are fatty acids stored?

A

As triglycerides

68
Q

What are glycolipids?

A

Sugar containing lipids with a sphingosine backbone

69
Q

What 2 things alter the melting point of a fatty acid chain?

A

The number of carbons in the chain increases the melting point

The number of double bonds reduces the melting point

70
Q

What are eicosanoids?

A

Chemical mediators (such as prostaglandins and thromboxanes) within the body derived from omega-3 and omega-6 fatty acids

Pharm Y1 (11 decks)

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