Chapter 4 Flashcards

1
Q

a (alpha) carbon

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2
Q

Amino Group

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3
Q

Carboxyl Group

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4
Q

Side Chain

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5
Q

R Group

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6
Q

Peptide Bond

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7
Q

Amino End

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8
Q

Carboxyl End

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9
Q

Polypeptide

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10
Q

Protein, residues

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11
Q

Primary Structure

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12
Q

Secondary Structures

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13
Q

Tertiary Structures

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14
Q

Quaternary Structure

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15
Q

Alpha Helix

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16
Q

Beta Sheet

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17
Q

Denatured

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18
Q

Chaperones

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19
Q

Translation

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20
Q

Messenger RNA (mRNA)

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21
Q

Ribosomes

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22
Q

A (aminoacyl) Site

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23
Q

P (peptidyl) Site

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24
Q

E (exit) Site

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25
Q

Codon

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26
Q

Reading Frames

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27
Q

Anticodon

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28
Q

Aminoacyl tRNA Synthetases

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29
Q

Genetic Code

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30
Q

Initiation

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31
Q

Elongation

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32
Q

Termination

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33
Q

Initiation Factors

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34
Q

Elongation Factors

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35
Q

Release Factor

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36
Q

Polycistronic mRNA

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37
Q

What are the major groups of amino acids as categorized by the properties of their R groups? How do the chemical properties of each group affect protein shape?

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38
Q

How do the peptide bonds, hydrogen bonds, ionic bonds, disulfide bridges, and noncovalent interactions (van der Waals forces and the hydrophobic effect) define a protein’s four levels of structure?

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39
Q

What ultimately determines the three-dimensional shape of a protein?

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40
Q

A mutation leads to a change in one amino acid in a protein. The result is that the protein no longer functions properly. How is this possible?

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41
Q

Which polypeptide sequence would you expect to result from a synthetic mRNA with the sequence 5’- UUUCCGAUGGGGUUUGGGUUUGGG-3’?

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42
Q

What are the steps of translation? Name and describe each one.

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