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Adv Bio - Proteins > Lesson Four - Levels of Protein Structure > Flashcards

Lesson Four - Levels of Protein Structure Flashcards

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Biology 101 flashcards
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

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2
Q

How many levels are there of protein structure?

A

Four

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3
Q

What is the Primary structure?

A

Simply the sequence of amino acids in a protein

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4
Q

Where are the chains of amino acids written from?

A

The amino terminus to teh carbxyl terminus

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5
Q

What are the two types of the secondary structure?

A

a-helix

b-sheet

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6
Q

What types of bonds are present is the secondary structure?

A

Hydrogen bonding

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7
Q

Explain a-helix

A

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

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8
Q

How many models are there of a-helix?

A

3

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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

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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

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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

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12
Q

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

A 
Hydrophobic interactions
Ionic bonds
Hydrogen bonds
LDF
Disulfide bridges
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13
Q

Which techniques can be used to identify a tertiary structure?

A

X-ray crystallography

NMR (nuclear magnetic resonance)

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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

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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

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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?

A

Cysteine

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
Q

Why do proteins fold?

A

To give a structure with the lowest free energy

26
Q

When would the structure of the protein change?

A

When there is a change in the chemical environment

27
Q

How does the temperature affect a protein molecule?

A

It increases the kinetic energy which places stress on bonds which breaks them

28
Q

What types of bonds are particularly susceptible to temperature in a protein?

A

Hydrogen bonds
Ionic bonds
Van der Waals

29
Q

What effect does pH have on a solution?

A

It changes the concentration of Hydrogen ions and hydroxide ions

30
Q

How does pH affect a protein?

A

It changes the relative charge of the protein and places stress on polar interactions s

31
Q

What does a change in temperature and pH result in?

A

It denatures the protein and causes the loss of tertiary structure and function

32
Q

What is a quaternary sturcture?

A

A protein which is made up of two or more polypeptide subunits

33
Q

What cell is an example of quaternary structure and why?

A

Haemoglobin as it is tetrameric

34
Q

What does tetrameric mean?

A

It is made up of 4 parts

35
Q

What is haemoglobin made up of?

A

2 a-helices and 2 b-sheets

36
Q

Some integral proteins can be…

A

Transmembrane

37
Q

What are some examples of transmembrane proteins?

A

Channels
Transporters
Receptors

38
Q

What type of protein are transmembrane?

A

Hydrophobic

39
Q

FINISH FLASHCARdS ON PERIPHERAL PROTEINS< JUNCTIONS BETWEEN CELLS +HIV

A

:)

Adv Bio - Proteins (6 decks)

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