Proteins (c) Protein Structure, Ligand binging and conformational change (i) Flashcards

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1
Q

Amino Acid sequence determines…

A

Protein structure

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2
Q

Proteins are…

A

Polymers of amino acid monomers

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3
Q

Amino acids link by…

A

Peptide bonds to form polypeptides

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4
Q

Amino acids have the same…

A

basic structures, differing only in the R group present

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5
Q

Amino acids are classified according to…

A

Their R groups: Basic (positively charged); acidic (negatively charged), polar; hydrophobic

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6
Q

The wide range of functions carried out by proteins results from…

A

The diversity of R groups

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7
Q

The primary structure is…

A

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

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8
Q

Hydrogen bonding along the backbone of the protein strand results in…

A

Regions of secondary structure: Alpha helices, parallel or anti-parallel beta sheets, or turns.

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9
Q

The polypeptide folds into a…

A

Tertiary structure

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10
Q

This conformation is stabilised by…

A

Interactions between R groups: hydrophobic interactions; ionic bonds; london dispersion forces; hydrophobic bonds; disulfide bridges.

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11
Q

Disulfide bridges are…

A

Covalent bonds between R groups containing sulfur.

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12
Q

Quaternary structures exist in proteins with…

A

Two or more connected polypeptide subunits

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13
Q

Quaternary structure describes the…

A

Spatial arrangements of the subunits.

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14
Q

A prosthetic group is…

A

A non-protein unit tightly bound to a protein neccessary for its function.

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15
Q

The ability of haemoglobin to bind oxygen is dependent on…

A

The non-protein haem group.

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16
Q

Interactions with the R groups can be influenced by…

A

Temperature and pH

17
Q

Increasing temperature disrupts the…

A

Interactions that hold the protein in shape; the protein begins to unfold, eventually becoming denatured.

18
Q

R groups of amino acids can vary in…

A

Size, shape, charge, hydrogen bonding capacity and chemical reactivity.

19
Q

The changes on acidic and basic R groups are affected by…

A

pH

20
Q

As pH increases or decreases from the optimum, the normal ionic interactions between charged groups are lost, which gradually changes the…

A

Conformation of the protein until it becomes denatured.