Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

ESA 1 - Medical Cell Biology & Genetics > Session 4.3c - Lecture 1 - Protein Structure > Flashcards

Session 4.3c - Lecture 1 - Protein Structure Flashcards

Slides 24-45

You may prefer our related Brainscape-certified flashcards:
USMLE® Step 1 flashcards AP® Biology flashcards Biology 101 flashcards
1
Q

Fill in the gaps using these words. They can be used more one once.

Function
Sequence
Structure

________ determines _________

_________ determines ________

A

Sequence determines structure

Structure determines function

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

Fig. 24

What does this image show?

A

A DNA binding protein with two lobed halves.

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

DNA has _____ and _____ grooves.

A

Major and minor grooves

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

What structure do we often find in many DNA binding molecules?

A

A helix turn helix motif

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

What is the significance of the helix turn helix motif in DNA binding molecules?

A

They wrap around DNA and they’re specifically designed to do that to make these tight interactions

DNA has major and minor grooves.

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

Draw a simplistic view of a DNA binding molecule.

A

DNA binding molecule with two lobes

DNA in centre

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

What is important in the folding of proteins?

A

The backbone sequence, i.e. the bonds formed between the different amino acid residues

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

What are the bonds formed between different amino acid residues?

A

Peptide bonds

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

Describe the movement related to and around the peptide bond?

A

Peptide bond is rigid and planar

We can get flexibility and rotation around the other bonds on either side of the peptide bond

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

What is the significance of the flexibility of bonds around the peptide bond?

A

These bonds determine the overall 3D structure

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

What is the protein conformation for primary structure?

A

Covalent (peptide) bonds hold primary structure together

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

How do psi and phi bonds contribute to the protein folding?

A

Angles determine the conformation of peptide backbone and hence the ‘fold’ of the protein

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

Fig. 25

Label the image

A 
- backbone
peptide plane
R1 R2 R3
- 1.45 A
- 1.33 A
- 1.52 A
- 1.23 A

118o
120o
122o

116o
121o
123o

Different angle determine the conformation of peptide backbone and hence hte ‘fold’ of the protein

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

Draw a schematic representation of the protein conformation of primary structure

A

See Fig. 25

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

Name a common secondary structure conformation.

A

Alpha-helix

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

What is an alpha helix?

A

It is a right-handed helix.

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

What is a right-handed helix?

A

If you hold you right hand up in a thumbs up, the helix follows the direction of your hand

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

How many amino acids does an a-helix have per turn?

A

3.6 amino acid residues per turn

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

What is the pitch of the a-helix?

A

Distance you go as you go up 1 amino acid residue

= 0.54 nm

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

Fig. 26

What does this image show?

A

Ribbon-like cartoon of an alpha helix (secondary structure of a protein)

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

Draw the outline of an alpha-helix of a protein (second structure)

[WOULD NOT HAVE TO DRAW]

A

See Fig. 26

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

What holds the alpha-helix secondary structure together?

A

By hydrogen bonds (H-bonds)

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

Where do the hydrogen bonds in the alpha-helix secondary structure come from?

A

Between the amide-hydrogen (N-H) and carbonyl-oxygen (C=O)

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

How is the alpha-helix secondary structure stabilised?

A

H-bonds between N-H and C=O stabilise the structure of the a-helix.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

Fig. 27

Label the bond and fill in the key

A
  • hydrogen bond
hydrogen (white)
carbon (grey)
nitrogen (blue)
oxygen (red)
R groups (purple)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

Draw the secondary structure a-helix of a protein and show how it is stabilised.

[WOULD NOT HAVE TO DRAW]

A

See Fig. 27

Alpha helix structure

hydrogen (white)
carbon (grey)
nitrogen (blue)
oxygen (red)
R groups (purple)

hydrogen bonds between N-H and C=O bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

Which amino acid residues are involved in the H-bond in alpha-helical secondary structure of proteins?

A

An interaction between 1 amino acid residue and 4 amino acids away.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

Fig. 28

Caption this image

A

Secondary structure - the a-helix

Flattened conformation showing the backbone -C=O group of one residue is H-bonded to the -NH group of the residue four amino acids away

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

Draw the secondary structure of the alpha-helix in a flattened conformation, explaining which amino acids interact.

[WOULD NOT HAVE TO DRAW]

A

See Fig. 28

Ri
Ri+1
Ri+2 etc.

Ri –> Ri+4
Ri+1 –> Ri+5

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

What affects the a-helix stability?

A

The amino acid sequence

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

Why does the amino acid sequence affect a-helix stability?

A

Not all polypeptide sequences adopt a-helical structures; certain ones are more likely to form them than others.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

Which residues are likely to form an a-helix?

A

Small hydrophobic residues such as Ala and Leu are strong helix formers

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

What is the significance of proline in a-helix stability?

A

Pro has its side chain bonded back into the amino group. This means it acts as a helix breaker because the rotation around the N-Ca bond is impossible (inflexible)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

What is the significance of glycine in a-helix stability?

A

Gly acts as a helix breaker because the tiny R-group supports other conformations

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

Which amino acids are strong helix formers, and which are helix breakers?

A

Formers = small hydrophobic residues e.g. Ala, Leu

Breakers = Pro, Gly

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

Other than a-helices, what is the other common secondary structure?

A

β-strand

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

What is the conformation of a β-strand?

A

It is a fully extended conformation (an extended conformation like you’ve stretched out the protein sequence)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

What is the distance between amino acids in β-strand conformation?

A

0.35 nm between adjacent amino acids (much more than we saw previously)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

Where are the R groups for β-strands?

A

They alternate between opposite sides of the chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

Fig. 30

What does this image show?

A

β-strand secondary structure of a protein (extended conformation)

0.35 nm between adjacent amino acids

R groups alternate between opposite sides of the chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

Draw a β-strand secondary structure conformation.

[WOULD NOT HAVE TO DRAW]

A

See Fig. 30

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

What do 2 β-strands form?

A

A β-sheet

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

What is a β-sheet made up of?

A

β-strands

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

β-_______ make up a β-_____ in the secondary structure of proteins.

A

β-strands make up a β-sheet

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q

How do two β-strands make a β-sheet?

A

2 β-strands come together in a side-by-side arrangement and stabilise themselves by forming Hydrogen bonds.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

How are β-sheets arranged?

A

Side-by-side antiparallel β-strands coming together

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

What stabilises a β-sheet?

A

Hydrogen bonds (between the β-strands)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

What is the general structure of β-sheets?

A

Antiparallel β-sheet or parallel β-sheet

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

What is an antiparallel β-sheet?

A

Adjacent β-strands run in opposite directions (i.e. one left to right and one right to left), with multiple inter-strand H-bonds stabilising the structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
50
Q

Fig. 31

Label this image.

A

Antiparallel β-sheet: adjacent β-strands run in opposite directions, with multiple inter-strand H-bonds stabilising the structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
51
Q

Draw an antiparallel β-sheet.

[WOULD NOT HAVE TO DRAW]

A

See Fig. 31

Yellow arrows: antiparallel
Boxes - show H-bonds between antiparallel β-sheets
Green lines - Hydrogen bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
52
Q

In an antiparallel β-sheet, where are the hydrogen bonds?

A

Between different strands

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
53
Q

How does an antiparallel β-sheet appear from a side view?

A

You can see a sort of ‘wavy’ pattern

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
54
Q

What is the key importance about antiparallel β-sheets?

A

The R groups are on opposite sides as we go through.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
55
Q

Fig. 32

Label and caption the image

A

(a) Antiparallel

Top view (top)

Side view (bottom)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
56
Q

Draw an antiparallel β-strand from top and side views.

[WOULD NOT HAVE TO DRAW]

A

1) Top - 3 β-strands on top of each other, stabilised by H-bonds. They run antiparallel to each other.
2) Side view - 3 β-strands forming a wavy pattern

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
57
Q

What is a parallel β-sheet?

A

Where the two strands go in the same direction.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
58
Q

Describe the H-bonds of a parallel β-sheet in comparison to that of an antiparallel β-sheet.

A

In a parallel β-sheet, the H-bonds are slightly kinked so they are not quite as strong.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
59
Q

Fig. 33

Label this image.

A

A parallel β-sheet

Strands are going in the same direction

H-bonds are slightly kinked (not as strong)

(Note: would not have to draw)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
60
Q

Fig. 34

Label this image.

A

Parallel β-sheet

Top view (strands going in the same direction, kinked H-bonds)

Side view (strands on top of each other, wavy pattern)

Same sort of pattern as antiparallel β-sheet

(Note: would not have to draw)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
61
Q

What is a mixed β-sheet?

A

Where β-strands run in all directions (some same, some opposite)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
62
Q

Some β-sheets have both antiparallel and parallel layers. What are these called?

A

A mixed β-sheet

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
63
Q

Fig. 35

Label this image.

A

Structure of a mixed β-sheet

Top two layers parallel (kinked H-bonds)

Bottom two layers antiparallel (strong H-bonds; straight)

(Note: would not need to draw)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
64
Q

How do we represent a-helices and β-sheets?

A

‘Cartoon’ versions:

a-helices: ribbon-like structure

β-strands/sheets: flat arrows

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
65
Q

What is the function of ferritin?

A

It is an iron storage protein

66
Q

Give an example of a protein that is largely a-helical in structure.

A

Ferritin

67
Q

Give an example of a protein that is largely β-stranded in structure.

A

Fatty acid binding protein

68
Q

Fig. 36 (Left)

Label this image.

A

Simple protein structure

Iron storage protein ferritin - largely a-helix

(Note: would not need to draw)

69
Q

Fig. 36 (Right)

Label this image.

A

Simple protein structure

Fatty acid binding protein - largely b-sheet

(Note: would not need to draw)

70
Q

In proteins, what does a ribbon-like coil represent?

A

A-helix

71
Q

In proteins, what does a flat arrow represent?

A

B-strand (which makes up b-sheets)

72
Q

What do a-helices and b-sheets fold up into?

A

The tertiary structure.

73
Q

What is the tertiary structure?

A

The overall 3D structure of the protein.

74
Q

What is myoglobin made up of (protein arrangement)?

A

Lots of a-helices (and ‘wiggly bits’)

75
Q

What does the tertiary structure show?

A

The spatial arrangement of amino acids far apart in the protein sequence.

76
Q

Fig. 37

Label this image.

A

Tertiary structure

Myoglobin

  • made up of a-helices
  • ‘wiggly bits’
  • purple = haem group bound to the molecule

The spatial arrangement of amino acids far apart in the protein sequence.

77
Q

What group binds to myoglobin?

A

Haem group

78
Q

What types of protein can you get?

A

Globular and fibrous proteins

79
Q

How big is a β-conformation

A

2000 X 5 A

80
Q

How big is an a Helix?

A

900 x 11 A

81
Q

How big are proteins generally in native globular form?

A

100 X 60 A

82
Q

What are the measurements of β-conformation, a Helix and Native globular forms?

A

β Conformation = 2000 X 5 A

a Helix = 900 x 11 A

Native globular form = 100 X 60 A

83
Q

What type of proteins are myoglobin and haemoglobin?

A

Globular proteins

84
Q

Which proteins are more biologically relevant: fibrous or globular proteins?

A

Globular proteins do more stuff/have more function

Fibrous proteins tend to be more simple in structure and function and are there to provide structural support

85
Q

What do globular proteins look like?

A

They are nicely folded up

86
Q

Carbonic anhydrase is an example of a globular protein. What secondary structure types does it contain?

A

A mixture - a helices, b sheets, b strands etc.

87
Q

Collagen is an important fibrous protein. What is its secondary structure like?

A

It has repeating structural motifs

88
Q

What is the role of a fibrous protein?

A

Support, shape and protection

89
Q

What is the role of a globular protein?

A

Catalysis, regulation

90
Q

What is the shape of a fibrous protein?

A

Long strands or sheets

91
Q

What is the shape of a globular protein?

A

Compact shape

92
Q

What type of secondary structure does a fibrous protein contain?

A

Single type of repeating secondary structure

93
Q

What type of secondary structure does a globular protein contain?

A

Several types of secondary structure

94
Q

Give an example of a fibrous protein.

A

Collagen

95
Q

Give an example of a globular protein.

A

Carbonic anhydrase

96
Q

Fig. 38 (top)

Label the images

A

β Conformation = 2000 X 5 A

a Helix = 900 x 11 A

Native globular form = 100 X 60 A

97
Q

Fig. 38 (bottom left)

Label the image

A

Collagen - Fibrous protein

(Fibrous proteins:

Role - support, shape, protection

Long strands or sheets

Single type of repeating secondary structure)

98
Q

Fig. 38 (bottom right)

Label the image

A

Carbonic anhydrase - Globular protein

(Globular proteins:

Role - Catalysis, regulation

Compact shape

Several types of secondary structure)

99
Q

What is collagen made up of?

A

3 alpha chains

(NOT a-helices; a-chains)

i.e. 3 polypeptide chains

100
Q

What do the constituents of collagen make up?

A

3 alpha chains make up a triple helical sequence

triple helical arrangement of collagen chains

101
Q

What sequence does collagen contain?

A

contain Gly - X - Y repeating sequence

Gly - any amino acid - any amino acid

102
Q

What stabilises the interactions between collagen chains?

A

Hydrogen bonds between chains stabilise helical structure.

103
Q

Give 3 facts about collagen.

A
  • Triple helical arrangement of collagen chains
  • Contain Gly - X - Y repeating sequence
  • Hydrogen bonds stabilise interactions between chains
104
Q

What do collagen molecules form?

A

Lots of collagen molecules come together to make a FIBRIL, which ultimately make a FIBRE.

105
Q

Collagen _________ come together to form a ______, which ultimately form a _____

A

Molecules
Fibril
Fibre

106
Q

What is a collagen fibre?

A

A BIG collagen structure made up of collagen fibrils (which are lots of collagen molecules)

107
Q

How does collagen appear under an electron microscope?

A

Striated, due to staining of collagen molecules

108
Q

How strong is collagen?

A

Really strong - stronger than steel

109
Q

What is the function of collagen?

A

Strong structural support (it is stronger than steel!); hence why it is a key part of bone and skin.

110
Q

Fig. 39 (top)

Label this image.

A

Collagen a chain

111
Q

Draw a collagen a chain.

A

See Fig. 39

112
Q

Fig. 39 (bottom)

Label this image.

A
  • Heavy staining in regions with gaps
  • Light staining in regions with no gaps
  • Staggered arrangement of collagen molecules causes the striated appearance of a negatively stained fibril
113
Q

What is negative staining?

A

Where the background is stained, so the actual specimen is untouched, and thus visible

(Positive staining = specimen stained)

114
Q

Draw a single collagen molecule,

A

See. Fig. 39 (bottom)

LEFT

115
Q

Draw the arrangement of collagen molecules in fibrils.

A

Staggered

See. Fig. 39 (bottom)
Second to left

116
Q

Draw a single collagen fibril under an electron microscope, and explain.

A

Striated

  • Light staining in regions with no gaps
  • Heavy staining in regions with gaps

See. Fig. 39 (bottom)
Second to right

117
Q

Draw how collagen fibrils look under an electron microscope, and explain.

A
  • Staggered arrangement of collagen molecules causes the striated appearance of a negatively stained fibril

See. Fig. 39 (bottom)
RIGHT

118
Q

What do globular proteins contain (structurally)?

A

A variety of tertiary structures, such as motifs and domains.

119
Q

What is a motif?

A

Folding patterns (repeating elements) containing 1 or more elements of secondary structure.

120
Q

Give 2 examples of motifs.

A

β-a-β loop

β-barrel

121
Q

What is a β-barrel?

A

A type of motif where beta strands form a ‘rounded’ shape.

122
Q

What are domains?

A

Part of a polypeptide chain that fold into a distinct shape. Often has a specific functional role.

123
Q

What is the difference between a domain and motif?

A

Domains tend to be bigger parts of a protein where they’re folded up into specific 3D shapes in their own right - big proteins will often have several different domains which will do different things.

124
Q

How can one protein do several different things?

A

Big proteins will often have several different domains which will do different things.

125
Q

Give an example of a protein that has 2 domains.

A

Troponin has got 2 rather similar shaped domains

126
Q

What is the role of troponin’s domains?

A

Bind calcium

127
Q

Why is the role of troponin’s domains important?

A

They bind calcium which is important for function of troponin in muscle contraction.

128
Q

Fig. 40 (left top)

Label the image.

A

β-a-β loop

129
Q

Fig. 40 (left bottom)

Label the image.

A

β-barrel

130
Q

Fig. 40 (right)

Label the image.

A

Calcium binding domains of troponin C

131
Q

What causes a protein to fold up?

A
  • Mainly due to ENTROPY

- Also so they can become the most stable form they can be (chemical properties)

132
Q

What does a space filling model of a protein show?

A

A better representation as we can see the nature of the amino acids that make it up.

133
Q

Which molecules do we get on the surface of water-soluble proteins?

A

Charged or polar molecules

134
Q

What do we find on the interior of a protein if we do a cross-section?

A

Hydrophobic residues

135
Q

Why do we find hydrophilic residues on the outside and hydrophobic residues in the middle?

A

Hydrophilic amino acid residues are on the outside interacting with water

Hydrophobic amino acid residues are in the middle packed away from water

136
Q

Describe the folding of water soluble proteins.

A

Polypeptide chains fold to so that hydrophobic side chains are buried and polar, charged chains are on the surface

137
Q

Fig. 41 (left)

Caption the image

A

Myoglobin

Ribbon diagram

138
Q

Fig. 41 (A)

Caption the image and provide a key

A

Myoglobin

(A) Space filling model

Blue = charged, yellow = hydrophobic, white = other

139
Q

Fig. 41 (B)

Caption the image and provide a key

A

Myoglobin

(B) Cross-section

Blue = charged, yellow = hydrophobic, white = other

140
Q

Describe the folding of membrane proteins.

A

Membrane proteins often show “inside-out” distribution of amino acids

141
Q

The middle of a membrane is very __________ due to ____________

A

The middle of a membrane is very hydrophobic due to lots of fatty acyl chains

142
Q

Give an example of a membrane protein.

A

Porins

143
Q

What do the hydrophobic residues interact with in porins?

A

Fatty acyl groups

144
Q

What do the hydrophilic residues interact with in porins?

A

Water-filled cavity

hydrophilic residues = charged/polar

145
Q

Fig. 42

Label the image.

A

Folding of membrane proteins, e.g. porins

  • Largely hydrophobic exterior
  • Water-filled hydrophilic channel
146
Q

Describe the folding of a water-soluble protein and the folding of a membrane protein and explain why.

A

Water-soluble proteins:

  • hydrophilic outside: interacts with water
  • hydrophobic inside: hidden from water

Membrane proteins:

  • hydrophobic outside: interact with fatty acyl chains
  • hydrophilic inside: interacts with water-filled cavity
147
Q

What is the quaternary structure?

A

Where we get further division - multi-subunit proteins

148
Q

Give an example of a protein structure where we have a quaternary structure from a protein of the same type.

A

Haemoglobin (has 4 subunits)

149
Q

What are the subunits of haemoglobin?

A

2 α subunits and 2 β subunits

150
Q

Give an example of a protein structure where we have a quaternary structure from interactions with other macromolecules.

A

Ribosome (has its own subunits and interacts with RNA molecules)

151
Q

What are the subunits of ribosome and what does it interact with?

A

55 protein subunits and 3 RNA molecules

forms an enormous complex

152
Q

What is the difference in quaternary structures of haemoglobin and ribosomes?

A

Haemoglobin has a quaternary structure from proteins of the same type

Ribosomes have a quaternary structure including interacts from other macromolecules.

153
Q

Fig. 43 (left)

Label the image.

A

Haemoglobin

2 α subunits and 2 β subunits

154
Q

Fig. 43 (right)

Label the image.

A

Ribosome

55 protein subunits and 3 RNA molecules

155
Q

What do I need to know?

  • Structure of an amino acid.
A

(Remember it is not about memorising detail but applying these things)

Need to know generalised amino acid structure

e.g. COO-, NH3+, R groups etc

156
Q

What do I need to know?

  • Properties of side chains of amino acids - how they are classified
A

(Remember it is not about memorising detail but applying these things)

Don’t need to know which ones are which, but if showed an amino acid to say its properties e.g. hydrophobic, charged etc.

e.g. OH - hydrophilic
alkanes - hydrophobic

157
Q

What do I need to know?

  • Why some amino acids are charged and how to calculate relative proportions
A

(Remember it is not about memorising detail but applying these things)

Why some side groups are charged (can be a difficult concept)!

e.g. pKa
pI
Henderson-Hasselbalch

158
Q

What do I need to know?

  • Structure and properties of a peptide bond
A

(Remember it is not about memorising detail but applying these things)

Need to know the features

e.g. Rigid
Planar
Flexibility around the peptide bond

159
Q

What do I need to know?

  • Features and properties of secondary structure - including why the properties of a peptide bond contribute to this
A

(Remember it is not about memorising detail but applying these things)

Some features of secondary structure, and very generally a-helix, b-sheet, why they’re important

e.g. a-helix
b-sheet
How sequences affect these

160
Q

What do I need to know?

  • What is meant by tertiary and quaternary structure
A

(Remember it is not about memorising detail but applying these things)

What we mean by them

e.g. tertiary = spatial 3D arrangement
quaternary = >1 subunit

161
Q

What do I need to know?

  • The types of bonds involved in maintaining protein structure
A

(Remember it is not about memorising detail but applying these things)

The types of bonds

e.g. peptide bond
H-bond
covalent bond

ESA 1 - Medical Cell Biology & Genetics (21 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions