Chapter 3.4: Proteins: Molecules with Diverse Structures and Functions Flashcards

1
Q

What are the seven functions of proteins?

A
  1. Enzyme catalysis
  2. Defense
  3. Transport
  4. Support
  5. Motion
  6. Regulation
  7. Storage
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2
Q

Define amino acid

A

the subunit structure from which proteins are produced, consisting of a central carbon atom with a carboxyl group (-COOH), an amino group (-NH2), a hydrogen, and a side group (R group); only the side group differs from one amino acid to another

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3
Q

What is the subunit structure from which proteins are produced, consisting of a central carbon atom with a carboxyl group (-COOH), an amino group (-NH2), a hydrogen, and a side group (R group); only the side group differs from one amino acid to another?

A

amino acid

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4
Q

Define peptide bond

A

the type of bond that links amino acids together in proteins through a dehydration reaction

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5
Q

What is the type of bond that links amino acids together in proteins through a dehydration reaction?

A

peptide bond

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6
Q

Define polypeptide

A

a molecule consisting of many joined amino acids; not usually as complex as a protein

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7
Q

What is a molecule consisting of many joined amino acids; not usually as complex as a protein?

A

polypeptide

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8
Q

Define primary structure

A

the specific amino acid sequence of a protein

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9
Q

What is the specific amino acid sequence of a protein?

A

primary structure

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10
Q

Define secondary structure

A

the bonding interactions between -CO and -NH groups of the primary structure

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11
Q

What is the bonding interactions between -CO and -NH groups of the primary structure?

A

secondary structure

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12
Q

Define alpha helix

A

a form of secondary structure in proteins where the polypeptide chain is wound into a spiral due to interactions between amino and carboxyl groups in the peptide backbone

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13
Q

What is a form of secondary structure in proteins where the polypeptide chain is wound into a spiral due to interactions between amino and carboxyl groups in the peptide backbone?

A

alpha helix

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14
Q

Define beta sheet

A

a form of secondary structure in proteins where the polypeptide folds back on itself one or more times to form a planar structure stabilized by hydrogen bonding between amino and carboxyl groups in the peptide backbone

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15
Q

What is a form of secondary structure in proteins where the polypeptide folds back on itself one or more times to form a planar structure stabilized by hydrogen bonding between amino and carboxyl groups in the peptide backbone?

A

beta sheet

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16
Q

Define tertiary structure

A

the folded shape of a protein, produced by hydrophobic interactions with water, ionic and covalent bonding between side chains of different amino acids, and van der Waal’s forces; may be changed by denaturation so that the protein becomes inactive

17
Q

What is the folded shape of a protein, produced by hydrophobic interactions with water, ionic and covalent bonding between side chains of different amino acids, and van der Waal’s forces; may be changed by denaturation so that the protein becomes inactive?

A

tertiary structre

18
Q

Define quaternary structure

A

the structural level of a protein composed of more than one polypeptide chain, each of which has its own tertiary structure

19
Q

What is the structural level of a protein composed of more than one polypeptide chain, each of which has its own tertiary structure?

A

quaternary structure

20
Q

Define motif

A

a substructure in proteins that confers function and can be found in multiple proteins

21
Q

What is a substructure in proteins that confers function and can be found in multiple proteins?

22
Q

Define domain (protein_

A

a distinct modular region of a protein that serves a particular function in the action of the protein

23
Q

What is a distinct modular region of a protein that serves a particular function in the action of the protein?

24
Q

Define chaperone protein

A

a class of enzymes that help proteins fold into the correct configuration and can refold proteins that have been misfolded or denatured

25
What is a class of enzymes that help proteins fold into the correct configuration and can refold proteins that have been misfolded or denatured?
chaperone protein
26
Define denaturation
the loss of the native configuration of a protein or nucleic acid as a result of excessive heat, extremes of pH, chemical modification, or changes in solvent ionic strength or polarity that disrupt hydrophobic interactions; usually accompanied by loss of biological activity
27
What is the loss of the native configuration of a protein or nucleic acid as a result of excessive heat, extremes of pH, chemical modification, or changes in solvent ionic strength or polarity that disrupt hydrophobic interactions; usually accompanied by loss of biological activity?
denaturation
28
Define dissaciation
in proteins, the reversible separation of protein subunits from a quaternary structure without altering their tertiary structure
29
What is in proteins, the reversible separation of protein subunits from a quaternary structure without altering their tertiary structure?
dissociation