Protein Structure, Ligand Binding And Conformational Change- Amino Acid Sequence Determines Protein Structure Flashcards

1
Q

What are proteins?

A

Polymers of amino acid monomers

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2
Q

What are amino acids linked by?

A

Peptide bonds to form polypeptides

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3
Q

How do amino acids differ in structure?

A

The R group present

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4
Q

What do R groups vary in?

A

-size
-shape
-charge
-hydrogen bonding capacity
-chemical reactivity

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5
Q

What are the different types of R group?

A

-basic (positively charged)
-acidic (negatively charged)
-polar
-hydrophobic

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6
Q

What happens as a result from diversity of R groups?

A

There is a wide range of different functions

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7
Q

What is the primary structure?

A

The sequence in which the amino acids are synthesised into the polypeptide

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8
Q

What is the secondary structure?

A

Hydrogen bonding along the backbone of the protein strand

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9
Q

What are the different types of secondary structures?

A

-Alpha helices
-Parallel or anti-parallel beta-pleated sheets
-turns

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10
Q

What is the tertiary structure?

A

The folded polypeptide

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11
Q

What is the conformation of the tertiary structure stabilised by?

A

Interactions between R groups

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12
Q

What are the different types of interactions between R groups?

A

-hydrophobic interactions
-ionic bonds
-ldf
-hydrogen bonds
-disulphide bridges (covalent bonds between R groups containing sulphur)

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13
Q

What is a quaternary structure?

A

They exists in proteins with two or more connected polypeptide subunits.

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14
Q

What does the quaternary structure describe?

A

The spatial arrangement of the subunits

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15
Q

What is a prosthetic group?

A

A non-protein unit tightly bound to a protein and necessary for it’s function

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16
Q

What is the ability of haemoglobin to bind oxygen dependent upon?

A

The non-protein haem group

17
Q

What can interactions of the R groups be influenced by?

A

Temperature and pH

18
Q

How is interactions of the R group influenced by temperature?

A

Increasing the temperature disrupts the interactions that hold the protein in shape, the protein then begins to unfold, eventually becoming denatured.

19
Q

How is interactions of the R group influenced by pH?

A

The charges on acidic and basic R groups are effectived by pH. As pH increases or decreases from the optimum the normal ionic interactions between charged groups are lost which gradually changes the conformation of the protein until it becomes denatured