proteins Flashcards

1
Q

the elements that are present in amino acids and proteins

A

Nitrogen, carbon, hydrogen, oxygen and some times sulfur

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2
Q

example of a role of a protein

A

haemoglobin transports oxygen around in the blood

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3
Q

what are the monomers which form proteins called

A

amino acids

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4
Q

what does the ‘R’ represent in the display formula of an amino acid

A

a carbon containing side chain

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5
Q

where do amino acids differ

A

in their side chain

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6
Q

what bond forms between two amino acids in a condensation reaction

A

peptide bond

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7
Q

other than the bond what forms by the condensation of two amino acids

A

a dipeptide

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8
Q

what parts of the amino acids react during a condensation reaction to form a dipeptide

A

the OH/hydroxyl group from one amino acid reacts with the hydrogen from the amine group of another to form the water molecule.

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9
Q

how are polypeptides formed

A

the condensation of many amino acids.

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10
Q

what is at each end of a peptide chain.

A

an amine group at one end and a carboxyl group at the other end.

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11
Q

four levels of organisation of proteins structure

A

primary, secondary,tertiary, Quaternary

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12
Q

describe the primary structure of a protein.

A

the sequence of amino acids in a polypeptide chain.

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13
Q

describe the secondary structure of a protein.

A

the folding of a polypeptide into an alpha helix or beta pleated sheet.

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14
Q

how is the structure maintained in the secondary structure of proteins.

A

hydrogen bonds between between the NH group of one amino acid and the c=o group of another.

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15
Q

describe the tertiary structure of a protein.

A

the further folding of the polypeptide chain into a specific 3D complex shape.

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16
Q

what determines how the polypeptide is folded in the tertiary structure of a protein.

A

the R group and the shape is held together between the R groups in different amino acids.

17
Q

three types of bonds between the R groups

A

Hydrogen bonds
ionic bonds- from between oppositely charged R groups
Disulphide bridges - covalent bonds which form between sulphur containing side chains.

18
Q

Why is the tertiary structure so important

A

the shape it forms determines how it reacts with other molecules e.g. active sites in enzymes

19
Q

what is quaternary protein structure

A

the structure of proteins which contains two or more polypeptide chains joined together.

20
Q

what is the chemical test for the presence of proteins

A

the biuret test - add biuret solution to the sample.
if the protein is present there will be a colour change from blue to lilac . If not present there will be no colour change.