Study guide 1 (pt 5) Flashcards

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1
Q

How many peptide bonds are formed in an oligopeptide of 4 amino acids?

A

3

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2
Q

How many water molecules are formed in the formation of 3 peptide bonds?

A

3

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3
Q

State the function of enzymatic catalysts

A

speed up reactions

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4
Q

A protein is a

A

biologically functional molecule made up of one more polypeptides

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5
Q

amino group, carboxyl group, alpha carbon and ‘R’ group.

A
H
             I
NH4+ - C - COO-
             I
         R group
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6
Q

There are _________ different amino acids in proteins

A

20

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7
Q

Which amino acids below will have an R group that is electrically charged at physiological pH?

A

serine, lysine, glutamic acid

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8
Q

Discuss how only 20 amino acids can be used to form a huge range of polypeptides.

A

they can be arranged in different combinations

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9
Q

The _________________ of amino acids determines primary structure of a protein

A

peptide bonds

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10
Q

bonds in secondary structure

A

hydrogen bonds

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11
Q

The union of _____________ or more polypeptides forms the _______________ structure.

A

two; quartinary

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12
Q

What molecule found in the nucleus determines the primary structure of a protein

A

sequence of DNA

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13
Q

Distinguish between the alpha helix and the beta-pleated sheet. What bond is responsible for these two structures?

A

alpha helix is coiled, beta pleated is straight

hydrogen bonds

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14
Q

List three types of non-covalent intermolecular forces that contribute to the tertiary structure of a protein.

A

hydrogen bonds, ionic bonds, hydrophobic interaction

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15
Q

Draw the disulfide bridge found in tertiary structure.

A

S-S

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16
Q

Define denaturation and explain how changes in pH and temperature lead to denaturation of proteins.

A

changes can cause the bonds to break and unfold the structure

17
Q

What bonds are notbroken in denaturation, even in irreversible denaturation?

A

peptide bonds