CH.4 Flashcards

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1
Q

misfolding of polypeptides is a serious problem in cells. Which of the following diseases are associated with accumulation of misfolded proteins?

A
  • Alzheimer’s
  • Parkinson’s
  • diabetes
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2
Q

the structural level of a protein least affected by a disruption in H bonding is the

A

primary level

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3
Q

what maintains the secondary structure of a protein

A

h-bonds

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4
Q

the function of each protein is a consequence of its specific shape. what is the term used for a change in three-dimensional shape on conformation Due to the disruption of hydrogen bonds, disulfide bridges, Or ionic bonds?

A

denaturation

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5
Q

there are 20 different amino acids. What makes one amino acid different from the other

A

different side chain groups ( R group)Attached to the alpha carbon

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6
Q

What would be an unexpected consequence of changing one amino acid in a protein consisting of 325 amino acid

A
  • the Primary structure of a protein would be changed
  • The tertiary structure of a protein would be changed
  • The biological activity or function of a protein might be altered
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7
Q

Which type of interaction stabilizes an alpha helixAnd beta-pleated sheets Structures of proteins?

A

H bonds

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8
Q

Which bonds are createdDuring the formation of the primary structure of a protein?

A

peptide bonds

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9
Q

Altering which levels of Structural organization could change the function of a protein

A
  • primary
  • secondary
  • tertiary
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10
Q

Finding two of the amino acid molecules to form a largerMolecule requires

A

The release of a water molecule

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11
Q

all of the following contain amino acids except

A

Cholesterol

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12
Q

what is the term used for A protein molecule that assist in the proper folding of another protein

A

chaperone

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13
Q

dehydration reactions are used in the forming of which of the following compounds

A
  • triacylglycerides
  • polysaccharides
  • proteins
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14
Q

The R group or side chain group of the amino acid serine -CH2-OH. The R group or side chain of Expect to find these amino acid alanine in a globular protein an aqueous solution

A

alanine Would be in the interior and serine Would be on the exterior of the globular protein

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15
Q

Upon chemical analysisA particular polypeptideWhat is found to contain 100 Amino acids.How many peptide bonds?

A

99

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16
Q

At which level of a protein Our interactions between the side chains(R groups) most important?

A

tertiary

17
Q

Polysaccharides lipids and proteins are similar in that they

A

Are synthesized by monomers by dehydration reactions

18
Q

The alpha helix and beta pleated sheet Are both common and polypeptide forms found in which protein level

A

Secondary

19
Q

Enzymes are

A

Proteins

20
Q

The tertiary structure of a protein is the

A

Unique three-dimensional shape of a fully folded polypeptide

21
Q

A strong covalent bond betweenAmino acids that functionsIn maintaining a polypeptide’s

A

disulfide bond

22
Q

What method did Frederick Sanger use to elucidate The structure of insulin?

A

Analysis of amino acid sequence of small fragments

23
Q

How many different kinds of polypeptides Each composed of 12 amino acids could be synthesized

A

2012

24
Q

the bonding of 2 aa molecules to form a larger molecule requires

A

the release/removal of a water molecule