proteins Flashcards

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1
Q

primary structure

(2)

A

-specific linear sequence of amino acids
- if one amino acid is changed in the sequence, it could render the protein dysfunctional

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1
Q

secondary structure

A
  • folds and coils at various locations of polypeptides due to hydrogen bonding in the polypeptide backbone
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2
Q

tertiary structure

(2)

A
  • 3D structure is determined by intermolecular reactions between R-groups in the polypeptide chain
  • (ionic bonds, hydrogen bonds, hydrophobic interactions, disulfide bridge
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3
Q

quarternary structure

A

some proteins consist of 2 or more polypeptide chains aggregated into one functional macromolecule

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4
Q

what is the basic structure of an amino acid

(5)

A
  1. a central carbon
  2. an amino group
  3. a carboxyl group
  4. an H atom
  5. a side chain (R)
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5
Q

how many amino acids are there

A

20/21

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6
Q

how many are essential

A

8/9

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7
Q

what type of reaction occurs in the synthesis of peptides? what type of bond is formed

A

dehydration and a peptide bond will form

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8
Q

polypeptide

A

a peptide with 50 or more amino acids linked together

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9
Q

protein

(2)

A
  • the most diverse and complex molecule in living organisms
  • it is a large molecule that consists of many amino acid subunit that are joined together by peptide bonds
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10
Q

how is a polypeptide different from a protein

A

a polypeptide is a chain of 50 or more amino acids and and a protein contains one or more polypeptides

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11
Q

denaturation

A

when a protein loses its 3-dimensional shape

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12
Q

what factors cause a protein to denature what are some examples

A
  • pH, temperature, salt
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13
Q

is denaturation irreversible, reversible or both? explain.

A

it is both because when removing the denaturing agent, it becomes reversible and when the peptide bonds are destroyed, denaturation becomes irreversible

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14
Q

amphiprotic

A

they possess both acidic and basic functional groups

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15
Q

beta pleated sheet

A
  • when two separate polypeptide strands run parallel to each other interact due to H bonds
16
Q

alpha helix

(2)

A
  • coiled shape
  • H bonds every 4th amino acid