Proteins Flashcards

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1
Q

What are some of the functions of proteins?

A

Enzymes, neurotransmitters, hormones, antibodies, transport, cell structure

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2
Q

What are the monomers of proteins?

A

Amino acids

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3
Q

Which elements are amino acids made from?

A

Carbon, hydrogen, oxygen, and nitrogen. Some also have sulphur.

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4
Q

What do we call two amino acids joined together?

A

A dipeptide

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5
Q

What do we call a long chain of amino acids?

A

A polypeptide

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6
Q

What are the four main parts of an amino acid?

A

Amino group, Alpha carbon (with H attached), Carboxyl group, Variable ‘R’ group

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7
Q

Which part of an amino acid is variable?

A

The ‘R’ group

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8
Q

How many different amino acids are there?

A

20

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9
Q

Amino acids can be joined together with which type of bond?

A

A peptide bond

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10
Q

Describe a peptide bond

A

A bond between two amino acids, between the nitrogen in the amine group of one amino acid and the carbon in the carboxyl group of the next

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11
Q

What type of reaction would form a peptide bond?

A

Condensation reaction (that releases water)

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12
Q

What type of reaction would break a peptide bond?

A

Hydrolysis reaction (that releases water)

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13
Q

What is the primary structure of a protein?

A

The sequence or order of amino acids in a polypeptide

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14
Q

Which bonds hold together the primary structure of a protein?

A

Peptide bonds

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15
Q

The function of a protein is determined by?

A

its shape

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16
Q

What is the secondary structure of a protein?

A

The folding of the primary structure into alpha helices or beta pleated sheets, held together by hydrogen bonds

17
Q

What type of bonds hold together the secondary structure of a protein?

A

Hydrogen bonds

18
Q

What is a hydrogen bond?

A

A weak bond between different molecules

19
Q

What is the tertiary structure of a protein?

A

The folding of the secondary structures into a precise 3D shape

20
Q

Which bonds hold together the tertiary structure of proteins?

A

Disulfide bonds (Very strong), Ionic bonds (Strong), Hydrogen bonds (Weak), Hydrophobic and hydrophilic interactions

21
Q

What is a disulfide bond?

A

A strong bond between cysteine amino acids (found in tertiary structure of proteins)

22
Q

What does hydrophilic mean?

A

Attracted to water

23
Q

What does hydrophobic mean?

A

Repels water

24
Q

What is the quaternary structure of (some) proteins?

A

When a protein is made of more than one polypeptide chain bonded together

25
Q

What is a prosthetic group on a protein?

A

A chemical group bonded to proteins, but not made of amino acids, such as the iron containing haem group in haemoglobin.

26
Q

What are globular proteins?

A

A common type of protein with a spherical shape that is normally soluble in water and has a variety of biological functions (eg enzymes, antibodies, hormones).

27
Q

What are fibrous proteins?

A

A common type of protein with a linear structure that is insoluble in water and provides a structural function (eg collagen and keratin)

28
Q

Describe the structure of haemoglobin

A

A globular protein with quaternary structure. It is made of four globular polypeptide chains.
Each polypeptide chain has one prosthetic group called haem. The haem contains an iron ion (Fe) which oxygen binds to.

29
Q

Describe the structure of collagen

A

It is a fibrous, insoluble protein. The fibrils are rigid/strong because of tightly coiled triple helices.
This gives strength across tissues because these fibrils can form cross-linkages to produce collagen fibres.

30
Q

Describe the role of haemoglobin

A

Haemoglobin is found inside red blood cells. It is used to transport oxygen around the body to be used in respiration.

31
Q

Describe the role of collagen

A

Collagen is found in large quantities in connective tissue throughout the body. It is very strong and its role is to support organs and bones.