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Introductory Biochemistry > Protein Structure > Flashcards

Protein Structure Flashcards

1
Q

Do peptide bonds have considerably more single or double bond character?

A

Double bond

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2
Q

Is a peptide bond closer in length to a double or single bond?

A

It is intermediate

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3
Q

Is there rotation around a single bond?

A

Yes

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4
Q

Is there rotation around a double bond?

A

No

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5
Q

The double-bond character of a peptide bond gives polypeptides what shape?

A

Planar

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6
Q

The polypeptide plane can only rotate at around what point in the chain?

A

By pivoting around the alpha-carbons at either side of the amino acids

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7
Q

When a protein folds, are the covalent bonds broken and reformed?

A

No

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8
Q

When a protein folds, is there a change in configuration and conformation?

A

There is no change in the configuration, but there is change in the conformation due to rotation around the covalent bonds

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9
Q

What is the primary structure of a protein?

A

The sequence of amino acids that are linked together to form a polypeptide chain

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10
Q

What is the secondary structure of a protein?

A

The local arrangement of the polypeptide chain in three dimensions. This arrangement is stabilised by intramolecular and sometimes intermolecular H-bonds between the amide groups

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11
Q

What are the two types of secondary structure?

A
  1. Alpha-helix
  2. Beta-sheets
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12
Q

Beta-sheets are made up of what?

A

Beta-strands

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13
Q

Is it the alpha-helix or the beta-sheets that have parallel or anti-parallel strands?

A

Beta-sheets

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14
Q

Parts of the polypeptide in a protein’s secondary structure are referred to as what?

A

Coil or omega-loops

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15
Q

Coils often form loops on what part of the protein?

A

The surface

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16
Q

What type of bonds are vital parts of secondary protein structures?

A

Hydrogen bonds

17
Q

What is the difference in H-bonds between alpha-helices and beta-sheets?

A

Alpha-helices contain intra-chain H-bonds and beta-sheets contain inter-chain H-bonds

18
Q

What is an example of a molecule with an alpha-helix secondary structure?

A

Myoglobin (made up mostly of alpha-helices)

19
Q

What is an example of a molecule with a beta-sheet secondary structure?

A

Immunoglobins (made up mostly of beta-sheets)

20
Q

What can proline residues do in a protein’s secondary structure?

A

Make/break helices

21
Q

What can threonine residues do in a protein’s secondary structure?

A

Stabilises the helix by longitudinal H-bonding

22
Q

What is a protein’s tertiary structure?

A

The 3D arrangement of the entire polypeptide chain and all of its secondary structures

23
Q

What is an example of a protein that has multiple functions?

A

Myosin in muscle contraction has structural and catalytic functions

24
Q

What are the different functional types of protein?

A
  1. Binding
  2. Regulatory
  3. Structural
  4. Catalytic/enzymes
  5. Transport
  6. Receptors
  7. Ion channels
25
Q

What are some examples of structural proteins?

A
  1. Keratin
  2. Collagen
  3. Tubulins
  4. Actin
26
Q

What are some examples of binding proteins?

A
  1. Haemoglobin
  2. Immunoglobins
  3. Insulin
  4. Hormone binding proteins
27
Q

What are some examples of catalytic proteins?

A
  1. DNA polymerase
  2. Alcohol dehydrogenase
  3. CYP2D6
  4. Trypsin
28
Q

Red blood cells are made up of what protein, and what type of protein is it?

A

Haemoglobin molecules, which are binding proteins

29
Q

What is a protein’s quaternary structure?

A

The association of several protein chains/subunits in a closely packed arrangement. Each of the subunits has its own primary, secondary, and tertiary structure

30
Q

What is a protein network?

A

A system of protein-protein interactions which allow us to understand complex biology

31
Q

What is polymorphism?

A

The occurrence of two or more clearly different morphs/forms of a molecule

Introductory Biochemistry (16 decks)

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