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

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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?

A

motif

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?

A

domain

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
Q

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

A

chaperone protein

26
Q

Define denaturation

A

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
Q

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?

A

denaturation

28
Q

Define dissaciation

A

in proteins, the reversible separation of protein subunits from a quaternary structure without altering their tertiary structure

29
Q

What is in proteins, the reversible separation of protein subunits from a quaternary structure without altering their tertiary structure?

A

dissociation