Protein structure (4) Flashcards

Semester 1 year 1

1
Q

What is the primary structure of a protein?

A

The linear sequence of amino acids in the polypeptide chain

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2
Q

What does the sequence of a polypeptide have?

A

Directionality

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3
Q

What is the secondary structure of a protein?

A

-folding of the polypeptide backbone into regular structures
-structures such as: alpha helix, the beta sheet, turns + loops
-generally stabilised by H bonding between amino acid residues

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4
Q

Describe the alpha helix

A

-coiled structure held together by H bonds
-right handed (can have left handed, but rare)
-often amphiphilic (amphipathic) - have both hydrophobic + hydrophilic character

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5
Q

Where do the hydrogen bonds form in an alpha helix?

A

Between the main chain C=O of residue i and the main chain N-H of residue i+4 (every 4th residue)

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6
Q

How many residues are there per turn in an alpha helix, how much rise is there and rotation per residue?

A

-3.6 residues per turn
-1.5A rise per residue
-100 degrees per rotation

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7
Q

What is the alpha helix terminator?

A

Proline:
-contains a secondary amine
-doesn’t support the helix geometry

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8
Q

Describe beta sheets

A

-constructed from 2 or more polypeptides H bonded to each other
-each strand is in a nearly extended conformation
-sheets can be constructed from mixed parallel + antiparallel strands
-contains beta turns

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9
Q

What characteristic can beta sheets have due to certain sequences?

A

Amphipathic character

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10
Q

Describe beta turns

A

-compact globular nature of many proteins requires reversal in the direction of polypeptide chains
-H bonds between C=O of i residue + N-H of i+3 residue

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11
Q

Describe the supersecondary structure

A

-molecules of secondary structural elements can be combined with other secondary structure elements or supersecondary structures
-combined using connecting loops
-forms tertiary structure of proteins

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12
Q

Describe the tertiary structure

A

-assembly of secondary structure elements into native protein structure
-elements of secondary structure are connected by remaining segments in amino acid sequence
-forms connecting loops
-loops can move, so are useful for function

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13
Q

What is the quaternary structure?

A

-assembly of polypeptide chain into multi-subunit structures
-subunits usually associate non-covalently

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14
Q

What is the subunit interface constructed from?

A

-H bonds
-buried hydrophobic residues
-sometimes disulfides

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15
Q

What is haemoglobin?

A

A tetramer of 2 identical alpha subunits + 2 identical beta subunits - hetero-oligomer

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16
Q

What are allosteric interactions?

A

In many multimeric proteins, the binding of a ligand to 1 subunit can alter the affinity of the other subunit

17
Q

What are domains?

A

-polypeptides of more than roughly 200 residues fold into 2 or more globular clusters
-each domain of a protein has a specific function

18
Q

Where are binding sites on proteins often found?

A

Occupy the clefts between domains

19
Q

Describe the structure of immunoglobulins

A

-made of a light + heavy chain that have disulfide bonds between them
-have hypervariable loops, which are often functionally important