Chapter 4 Flashcards

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1
Q

α helix only

A
  1. Cylinder Structure

2. One full turn every 3.6 amino acids

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2
Q

β sheet only

A
  1. Consists of antiparallel or parallel strands

2. Side Chains alternating above and below the structure

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3
Q

Both α helix & β sheet

A
  1. Can be formed by many sequences

2. Formed by hydrogen-bonding between backbone atoms

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4
Q

The antibody is composed by __ polypeptide chains

A

4

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5
Q

If SDS-PAGE were used for a pure sample of this protein that was preincubated with mercaptoethanol, then there would be __ bands expected.

A

2

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6
Q

How do most motor proteins ensure their movements are unidirectional?

A

They couple a conformational change to the hydrolysis of an ATP molecule.

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7
Q

A disulfide bond is a ___ interaction within the protein.

A

covalent

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8
Q

Protein molecules that have a quaternary structure must have two or more of which of the following?

A

polypeptide chains

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9
Q

What is the definition of a protein-binding site?

A

any region on a protein’s surface that interacts with another molecule through “noncovalent” bonding.

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10
Q

What are protein families?

A

Evolutionary related proteins that are similar in amino acid sequence and three-dimensional conformation.

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11
Q

In a globular protein, where would the amino acid tryptophan most likely be found?

A

buried in the protein’s interior

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12
Q

What does the primary structure of a protein refer to?

A

The linear amino acid sequence of the protein.

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13
Q

What do the segments of a transmembrane protein that cross the lipid bilayer usually consist of?

A

an α helix with mostly nonpolar side chains

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14
Q

For which reason are α helices and β sheets common folding patterns in polypeptides?

A

The amino acid side chains are not directly involved in their formation.

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15
Q

The protein can be unfolded by a process called ____

A

Denaturation

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16
Q

Generally speaking, what determines the biological activity of a protein?

A

amino acid sequence.

17
Q

What provides the information necessary to specify the three-dimensional shape of a protein? Choose the best answer in the context of which generally applies to most proteins.

A

protein’s amino acid sequence.

18
Q

Which part of an amino acid gives it its unique properties?

A

side chain.

19
Q

Which part of amino acids are involved in a peptide bond?

A

amino group of one amino acid and carboxyl group of the other.

20
Q

Hydrogen bonding between N-H and C=O groups of every fourth amino acid within a polypeptide chain results in which type of folding pattern?

A

a helix

21
Q

A stretch of amino acids in a polypeptide chain that is capable of independently folding into a defined sturcture is called a ____

A

domain

22
Q

A binding site on the surface of a protein interacts specifically with another protein through___

A

many weak noncovalent interactions.

23
Q

How does phosphorylation of a protein affect its activity?

A

It could increase or decrease activity.

24
Q

How many amino acids are commonly used in making proteins?

A

20

25
Q

Which parts of amino acids are involved in a peptide bond?

A

amino group of one amino acid and carboxyl group of the other

26
Q

Which part of an amino acid gives it its unique properties?

A

side chain (R group in protein)

27
Q

What is the best type of model for visualizing the surface of a protein?

A

space-filling

28
Q

What are the two types of β sheets?

A

parallel and antiparallel

29
Q

What does the primary structure of a protein refer to?

A

The linear amino acid sequences of the protein.

30
Q

Consider the thermodynamic properties of chemical reactions. Even though enzymes do not affect the overall energy of the reactants or the products (i.e., the thermodynamics), they alter the speed of the reaction. Enzymes accomplish this by doing which of the following?

A

reducing the activation energy of a reaction

31
Q

For a given protein, hydrogen bonds can form between which of the following?

A
  1. atoms in the polypeptide bacbone
  2. atoms of two peptide bonds
  3. atoms in two side chains
  4. a side chain and water.
32
Q

How does an allosteric inhibitor work?

A

It binds to a site other than the active site, causing a conformational change in the enzyme that makes the active site less accommodating to the substrate.

33
Q

How does phosphorylation control protein activity?

A

The phosphate group induces a change in the protein’s conformation.

34
Q

What kind of enzyme adds a phosphate group to another protein?

A

kinase

35
Q

What kind of enzyme removes a phosphate group from a protein?

A

phosphatase

36
Q

In an α helix, hydrogen bonds form between which of the following?

A

every fourth amino acid.