The Patient Semester 1 Flashcards

(70 cards)

1
Q

Which amino acid has the following side chain?

A

Glycine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Which amino acid has the following side chain?

A

Methionine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

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

A

Proline

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Which amino acid has the following side chain?

A

Alanine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Which amino acid has the following side chain?

A

Valine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Which amino acid has the following side chain?

A

Isoleucine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Which amino acid has the following side chain?

A

Lysine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Which amino acid has the following side chain?

A

Arginine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Which amino acid has the following side chain?

A

Histidine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Which amino acid has the following side chain?

A

Aspartate/Aspartic Acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Which amino acid has the following side chain?

A

Glutamate/Glutamic Acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Which amino acid has the following side chain?

A

Tyrosine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Which amino acid has the following side chain?

A

Phenyl Alanine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Which amino acid has the following side chain?

A

Threonine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Which amino acid has the following side chain?

A

Serine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Which amino acid has the following side chain?

A

Cysteine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Which amino acid has the following side chain?

A

Aspargine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Which amino acid has the following side chain?

A

Glutamine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Which amino acid has the following side chain?

A

Tryptophan

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Which amino acid has the following side chain?

A

Leucine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Which amino acid has two chiral centres?

A

Isoleucine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

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

A

50 or more

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Approximately how many different proteins does one cell contain?

A

>10,000

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

What percentage of dry cell weight do proteins account for?

A

>50%

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Which of the -L or -R isomers exist naturally in amino acids?
Only the -L form Spelling out CORN in a clockwise direction when the hydrogen is drawn as a forward wedge.
26
What rotation an occur aroud the alpha-carbon atom and what are the torsion angles known as?
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
27
What kind of reaction joins two alpha-amino acids together?
Condensation- removal of water
28
In which part of the cell do amino acids join together to form a peptide?
The ribosomes
29
In what direction is a polypeptide sequence written?
From the N-terminus to the C-terminus
30
How long should a single C-N bond measure?
1.49 angstrom
31
How long should a double C=N bond measure?
1.27 angstrom
32
What is the actual length of a C-N bond within a peptide? And why?
The actual length is 1.32 angstrom. This is because C-N behaves partially like a double bond due to resonance stabilisation.
33
Why is the peptide bond planar?
Due to restricted rotation around the C=O bond.
34
Which two amino acids have non-polar side chains?
Methionine Proline
35
Which three amino acids have basic side chains?
Lysine Arginine Histidine
36
Which two amino acids have acidic side chains?
Aspartate Glutamate
37
Which three amino acids have aromatic side chains?
Tyrosine Phenylalanine Tryptophan
38
Which five amino acids have hydrophillic side chains but are neutral?
Serine Threonine Asparagine Glutamine Cysteine
39
Which amino acid can form S-S bonds? And where can they form?
Cysteine can form S-S bonds interchain and intrachain, altering the overall protein shape.
40
What are the two most common secondary structures of amino acids?
Alpha-helixes Beta-strands
41
Approximately how long is a hydrogen bond within a protein structure?
~2.2-3.5 angstrom
42
What torsion angles give an alpha-helix?
phi- 57 psi- 47
43
How many residues are there per turn in an alpha-helix?
3.6
44
Which -NH does the -CO of an amino acid form a hydrogen bond with?
The -NH of the 4th residue ahead
45
What are the four main features of an alpha-helix?
R groups extend on the outside It twists clockwise Peptide bonds are planar Peptide bonds are trans
46
How are polypeptide coils formed?
Alpha-helices wind around eachother, they are extremely stable
47
How many amino acids must be present to form a Beta sheet?
At least 5
48
What are the three main observations in parallel Beta-sheets?
R groups point up and down Strands are held together by Hydrogen bonding between strands Both strands run from the N-terminus direction
49
What makes antiparallel B-sheets different to parallel ones?
In antiparallel sheets, the strands run in opposite directions
50
How many types of Beta turns are there? And what are they used for within a peptide?
There are two types and they are used to change direction
51
What are the two types of turn within a polypeptide and what are their characteristics?
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
What are the three levels of structrure complexity?
Motifs- arrangement of two of more secondary structural elements Domain- many folded motifs giving stable, self contained structure Subunit- combining many domains
53
What are the features of a disulphide bond?
Covalent and occur via oxidation 2.2 angstroms in length 167kJ/mol in strength
54
What is the strength of a hydrogen bond inside protein?
2-7kcal/mol in strength
55
What is the formula for Gibbs Free Energy? What does it measure?
A negative delta G means that it is stable.
56
What is the strength of the van der Waals forces in each C-H within a hydrocarbon?
8.4kJ/mol
57
What is the average strength of a hydrophobic bond within a protein?
4kJ/mol
58
What is the main driving force for protein binding/folding in aqueous solution?
The increased entropy of water as hydrophobic groups bury inside
59
What is glycolysis?
Anaerobic degradatin of glucose to produce ATP and pyruvate, occurs in the cytosol
60
What is the size of a prokaryotic cell?
1-5 micrometers in diameter
61
What is the size of a eukaryotic cell?
10-100 micrometers in diameter
62
How do ribosomes vary from prokaryotes to eukaryotes?
In eukaryotes they are 80S in size In prokaryotes they are 70S in size In eukaryotic organelles they are 70S
63
What is the thickeness of a membrane?
6-10nm
64
What is the basic structure of a phosphoglyceride?
65
What are phosphogylcerides derived from?
Glycerol or sphingosine
66
Define monounsaturated.
Contain only one double bond
67
How are fatty acids stored?
As triglycerides
68
What are glycolipids?
Sugar containing lipids with a sphingosine backbone
69
What 2 things alter the melting point of a fatty acid chain?
The number of carbons in the chain increases the melting point The number of double bonds reduces the melting point
70
What are eicosanoids?
Chemical mediators (such as prostaglandins and thromboxanes) within the body derived from omega-3 and omega-6 fatty acids