Lesson Four - Levels of Protein Structure Flashcards

(39 cards)

1
Q

What are the levels of protein structure?

A

Primary - amino acid sequence
Secondary - regular sub structures (alpha helix or beta sheets
Tertiary - 3D structure
Quaternary - Complex of protein molecules

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

How many levels are there of protein structure?

A

Four

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

What is the Primary structure?

A

Simply the sequence of amino acids in a protein

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

Where are the chains of amino acids written from?

A

The amino terminus to teh carbxyl terminus

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

What are the two types of the secondary structure?

A

a-helix

b-sheet

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

What types of bonds are present is the secondary structure?

A

Hydrogen bonding

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

Explain a-helix

A

The helix is right-handed with 4 residues (amino acids) per ture

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

How many models are there of a-helix?

A

3

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

What are the models of a-helix?

A

Ball and stick
The ribbon and then those combined
Hydrogen bonds between oxygen and hydrogen stabiles the helix

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

Explain b-sheets

A

Can be parallel or antiparallel

The different parallels will have different structures and hence different hydrogen bonds in different places

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

What is the Tertiary Structure?

A

It is all about the interactions between the R groups

This involves the folding of the polypeptide chains to give a more complex 3D structure

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

What interactions can be found within the R-groups in tertiary structure?

A
Hydrophobic interactions
Ionic bonds
Hydrogen bonds
LDF
Disulfide bridges
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Which techniques can be used to identify a tertiary structure?

A

X-ray crystallography

NMR (nuclear magnetic resonance)

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

Where about in a molecule does the non-polar R groups tent to be placed?

A

In the centre

They are classically found embedded in the phospholipid bilayer of a cell

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

What do hydrophobic and hydrophilic interactions influence and why?

A

The location of cellular proteins
R-groups at surface of a protein determine its location within a cell. Hydrophilic R groups will predominate at the surface of a soluble protein, hydrophobic R groups may cluster at the centre to form a globular structure

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

What are disulphide bonds/bridges?

A

Strong covalent bonds which can form between -SH groups

17
Q

Which amino acid contains the -SH group?

18
Q

What are prosthetic groups?

A

They are associated non-protein groups

19
Q

Where are prosthetic groups found?

A

Within some proteins

20
Q

Name four types of prosthetic groups

A

Haeme
Carbohydrate
Lipid
Nucleic Acid

21
Q

What is myoglobin?

A

A red protein containing haem, which carries and stores oxygen in muscle cells. It is structurally similar to a subunit of haemoglobin.

22
Q

How is myoglobin held together and what does it contain?

A

By a-helices which link together with nonhelical sections

It contains a haeme groups that is protected in a hydrophobic pocket

23
Q

How are protein structures held together in a tertiary structure?

A

By weak hydrogen bonds and a few disulphide bonds

24
Q

Why are tertiary structure proteins surprisingly stable?

A

As in the most part to the evolution of proteins that have useful yet stable conformations

25
Why do proteins fold?
To give a structure with the lowest free energy
26
When would the structure of the protein change?
When there is a change in the chemical environment
27
How does the temperature affect a protein molecule?
It increases the kinetic energy which places stress on bonds which breaks them
28
What types of bonds are particularly susceptible to temperature in a protein?
Hydrogen bonds Ionic bonds Van der Waals
29
What effect does pH have on a solution?
It changes the concentration of Hydrogen ions and hydroxide ions
30
How does pH affect a protein?
It changes the relative charge of the protein and places stress on polar interactions s
31
What does a change in temperature and pH result in?
It denatures the protein and causes the loss of tertiary structure and function
32
What is a quaternary sturcture?
A protein which is made up of two or more polypeptide subunits
33
What cell is an example of quaternary structure and why?
Haemoglobin as it is tetrameric
34
What does tetrameric mean?
It is made up of 4 parts
35
What is haemoglobin made up of?
2 a-helices and 2 b-sheets
36
Some integral proteins can be...
Transmembrane
37
What are some examples of transmembrane proteins?
Channels Transporters Receptors
38
What type of protein are transmembrane?
Hydrophobic
39
FINISH FLASHCARdS ON PERIPHERAL PROTEINS< JUNCTIONS BETWEEN CELLS +HIV
:)