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IMMS > Protein Structure > Flashcards

Protein Structure Flashcards

1
Q

What are properties of the peptide bond?

A

Very stable
Cleaved by proteolytic enzymes
Partial double bond
Flexibility around C atoms

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2
Q

What is the ‘backbone’?

A

A line following the peptide bonds

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3
Q

What is a ‘cartoon’?

A

A representation showing the fundamental secondary structures

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4
Q

What forces hold proteins together?

A

Van der Waals
Hydrogen bonds
Hydrophobic forces
Ionic bonds
Disulphide bonds

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5
Q

What are Van der Waals?

A

Weak attractive interactions between atoms due to fluctuating electrical charges.

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6
Q

What are hydrogen bonds?

A

Interaction between dipoles, involving a hydrogen and a oxygen/nitrogen

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7
Q

What are hydrophobic forces?

A

Uncharged and non-polar side chains

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8
Q

What are ionic bonds?

A

Occur between fully or partially charged groups

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9
Q

What are disulphide bonds?

A

Bonds between cysteine

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10
Q

What is the primary structure?

A

Linear sequence of amino acids linked by peptide bonds

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11
Q

What is the secondary structure?

A

Bonds forming between the primary structure, hydrogen bonds etc…

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12
Q

What is the alpha helix?

A

Hydrogen bonds between each carbonyl group

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13
Q

What is the beta sheet?

A

Hydrogen bonds between linear regions of polypeptide chains
Parallel or anti parallel sheets

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14
Q

What is the tertiary structure?

A

The overall 3D conformation of the protein?

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15
Q

What is the quaternary structure?

A

3D structure of a protein composed of multiple subunits
Same non-covalent interactions as tertiary structures

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16
Q

How to determine the structure of a protein?

A

Crystallography
X-ray diffraction

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17
Q

What are enzymes?

A

Biological catalysts, accelerate a reaction and provide a way to regulate the rate of reactions

18
Q

What enzymes are used to indicate liver function?

A

Acid phosphatase
Alanine aminotransferase

19
Q

What enzymes are used to indicate prostate cancer?

A

Alkaline phosphatase

20
Q

What enzyme is used to indicate pancreas function?

A

Amylase

21
Q

What enzyme is used to indicate renal function?

A

Angiotensin converting enzyme

22
Q

What enzyme is used to indicate liver function?

A

Aspartate aminotransferase

23
Q

What enzyme is used to detect muscle damage or myocardial infarction?

A

Creatinine kinase

24
Q

What factors influence haemoglobin saturation?

A

Temperature
H+
P CO2

25
Q

What is sickle cell anemia?

A

Genetic disorder characterised by the formation of hard, sticky, sickle shaped red blood cells

26
Q

What is sickle cell caused by?

A

Single nucleotide mutation
From GAG to GTG

27
Q

What is glutamic acid in haemoglobin substituted for?

A

Valine

28
Q

At what condition is the haemoglobin in sickle cell affected?

A

Low oxygen concentration

29
Q

With the eradication of malaria in some geographical areas, why does sickle cell trait persist in the population at such a high frequency?

A

It takes many generations to change gene frequencies

30
Q

What is truncation?

A

Premature termination, stop code where it doesn’t belong

31
Q

What is substitution?

A

Changing the amino acids

32
Q

What is Conservative substitution?

A

Amino acid is changed with a similar amino acid, charged with charged, hydrophilic with hydrophilic etc…

33
Q

What is Non-conservative substitution?

A

Mutation causes a completely different amino acid to be inserted

34
Q

What are deletions?

A

When part of the protein is removed, or stops

35
Q

What is misplacing?

A

When RNA is edited incorrectly, instead of removing an intron it carries on

36
Q

What are immunoglobulins?

A

Antibodies, produced to bind to antigens typically toxins or proteins on the surface of microbial agents

37
Q

What structure do antibodies have?

A

Beta sheets

38
Q

How do antibodies bind to antigens with high affinity?

A

Close proximity of the antibody CDR regions and the antigen surface
Intimate contact allows the combination of relatively weak interactions to produce a strong binding surface

39
Q

What is the portion of antigen bound known as?

A

Epitope

40
Q

What forces are used for the antigen-antibody bind?

A

Van der Waals
Hydrogen bonds

41
Q

What factors affect complementarity

A

Van der Waals
Hydrogen bonds
Charge
Bulk
Hydophobicity

IMMS (32 decks)

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