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Biology > Biology Exam 4 > Flashcards

Biology Exam 4 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

Describe general amino acid and protein structure.

A

Proteins are a polymer of amino acids held together by a peptide bond.
Amino acid- central carbon with amino groupp , carboxyl group, proton, r group

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2
Q

What are the four levels of protein structure?

A

Primary 1°
Secondary 2°
Tertiary 3°
Quaternary 4°

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3
Q

Describe peptide bond.

A

covalent bond between two amino acids

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4
Q

Describe protein modification.

A

phosphorylation - changes charge; on/off switch for enzyme
glycolsylatoin - makes it slippery
lipidizatoin; adds lipid becomes part of a membrane; peripheral or lipid linked
Ubiquination: adds ubiquitin to protein to send to proteasome.

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5
Q

Describe role of proteasome and protein degradation in the cell.

A

Ubiquinated proteins are send to the proteasome for cleavage and recycling.

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6
Q

What are the nine main categories of proteins.

A
  1. Enzymes
  2. Regulatory Proteins
  3. Structural Proteins
  4. Motility Proteins
  5. Transport Proteins
  6. Receptor Proteins
  7. Hormonal Proteins
  8. Defensive Proteins
  9. Storage Proteins
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7
Q

Explain how environmental factors affect protein folding and function.

A

Changes in temperature, pH, and salt concentration disrupts the stabilizing bonds within protein structure. This causes the protein to unfold and become denatured.

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8
Q

Define and identify: coding/non coding, template/non template DNA strands.

A
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9
Q

Describe all function of RNA polymerase.

A
  1. Binds the promotor
  2. Melts hydrogen bonds (unwinds promotor)
  3. Unwinds DNA front of bubble
  4. Synthesizes RNA 5 -> 3
  5. Rewinds DNA at back of bubble
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10
Q

What are the three stages of transcription.

A
  1. Initiation
  2. Elongation
  3. Termination
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11
Q

Explain why wobble allow for 64 codons.

A

the third position does alternative base pairing allows it to have multiple codon targets

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12
Q

Explain role of signal sequences in protein targeting.

A

Signal sequences are located on the N-terminus of some proteins and enable those proteins to find their correct location

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13
Q

Describe primary protein structure.

A
  • a sequence of amino acids
  • synthesized and read from n-terminus to c-terminus
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14
Q

Describe secondary protein structure.

A
  • 3D arrangement of the primary sequence
  • alpha helix or beta helix
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15
Q

Describe tertiary protein structure.

A

3D arrangement of secondary structure
- Globular Proteins
- Fibrous Proteins
- Transmembrane Proteins

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16
Q

Describe quaternary protein structure.

A
  • 3D arrangement of polypeptides in a multi subunit protein complex (2 proteins interacting to be functional)
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17
Q

What is the function of enzymes?

A
  • Catalyze chemical reactions (make bond, break bond)
  • Bind substances and convert them into products
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18
Q

What is the function of regulatory proteins?

A
  • Bind enzymes and control their functions.
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19
Q

What is the function of structural proteins?

A

Structural support to cells and tissues

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20
Q

What is the function of motility proteins?

A
  • Interact with structural proteins to generate motion
  • Can move individual proteins, vesicles, organelles, chromosomes, or larger structures
  • Movement requires energy: often bind ATP
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21
Q

What is the function of transport proteins?

A
  • Control movement of small molecules across membranes
  • Always found in membranes
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22
Q

What is the function of receptor proteins?

A
  • Bind to signaling molecules (including molecules)
  • In membrane and cytosol
  • Bind to signal and pass it on
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23
Q

What is the function of hormonal proteins?

A
  • Chemical signals between cells in multicellular organisms
  • Circulate to distant cells
  • Bind cell surface receptors on target cells
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24
Q

What is the function of defensive proteins?

A
  • Target and neutralize harmful molecules
  • Ex: antibodies
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25
Q

What is the function of storage proteins?

A
  • Bind to and protect energy sources
  • Facilitate long-term storage of energy molecules
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26
Q

What is the shape of a fibrous protein?

A

Long and Narrow

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27
Q

What is the purpose of a fibrous protein?

A

structural

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28
Q

What is the amino acid sequence of a fibrous protein?

A

repetitive

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29
Q

What is the durability of a fibrous protein?

A

Less sensitive to changes in pH and temperature

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30
Q

What is an example of a fibrous protein?

A

Nuclear laming, collagen, fibrin, keratin

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31
Q

What is the solubility of a fibrous protein?

A

(Generally) insoluble in water

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32
Q

What is the shape of a globular protein?

A

Round/spherical

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33
Q

What is the purpose of a globular protein?

A

Functional

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34
Q

What is the amino acid sequence of a globular protein?

A

Irregular

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35
Q

What is the durability of a globular protein?

A

More sensitive to changes in pH and temperature

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36
Q

What is an example of a globular protein?

A

Histones, enzymes, hemoglobin, insulin

37
Q

What is the solubility of a globular protein?

A

(Generally) soluble in water

38
Q

What is the structure of an alpha helix?

A
  • 3.6 amino acid per turn
  • stabilized by hydrogen bonds between every 4th amnio acid
  • R-groups extend outward uninterrupted sequence of amino acids
39
Q

What is the structure of a beta sheet?

A
  • stabilized by hydrogen bonds in polypeptide backbone
  • bonds form between aligned strands
  • parallel or anti parallel
  • Strands in sheet are separated by loops that allow chain to curve around
40
Q

What determines protein shape?

A

amino acid sequence

41
Q

Are non polar amino acids hydrophobic or hydrophilic?

A

hydrophobic

42
Q

Are polar amino acids hydrophobic or hydrophilic?

A

hydrophilic

43
Q

Are ionic amino acids hydrophobic or hydrophilic?

A

hydrophilic

44
Q

What determines protein function?

A

Shape

45
Q

How many amino acids are in an average protein?

A

300-500

46
Q

What hold amino acids together?

A

peptide bonds

47
Q

Are most peptide bonds in the trans or Cis configuration?

A

trans

48
Q

Is protein structure regular or predictable?

A

no

49
Q

What is a beta barrel?

A

A large enough beta sheet that can fold into a beta barrel

50
Q

Characteristics of a globular protein?

A
  • condensed, rounded
  • hydrophobic amino acids inside, hydrophilic outside
51
Q

Characteristics of fibrous proteins?

A
  • rich in a- helices and b-sheets
  • resistant to mechanical force (STRONG)
52
Q

Characteristics of transmembrane proteins?

A
  • span membrane
  • transmit info across membrane
  • Ex: signaling receptors
53
Q

What is a domain?

A

subsection of a protein with a particular function (section of protein)

54
Q

Unfolded 1degree structure

A

peptide

55
Q

folded functional 3degree structure

A

protein

56
Q

What is ubiquination?

A

bonding of an ubiquitin protein to a protein which acts as a signal to destroy that protein

57
Q

What is the function of phosphorylation for a protein?

A

on/off with for an enzymes; adds phosphate group to protein

58
Q

What is the function of glycosylation for a protein?

A

addition of a sugar to the protein; makes cell slippery so they can move past each other

59
Q

What is the function of farnelyaition for a protein?

A

adds a lipid molecule to the protein

60
Q

What factors change protein shape?

A
  • Environmental change
  • Covalent modification
  • Non covalent modification
61
Q

What maintains the circadian clock?

A

protein degradation

62
Q

What occurs in transcription initiation?

A
  • RNA polymerase binds to the promotor sequence
  • RNA pol melts promotor DNA
  • RNA pol begins synthesis without a primer
63
Q

How does RNA pol find a promotor sequence?

A

looks for a particular sequence

64
Q

What occurs in transcription elongation?

A
  • RNA pol makes an RNA strand complementary to the template DNA in a 5 to 3 direction
  • only one strand of DNA gets copied
65
Q

What occurs in transcription termination?

A
  • RNA pol reaches termination sequence
  • RNA pol pauses
  • mRNA folds up into a hair-pin loop or Rho protein binds
  • RNA pol release DNA and RNA
66
Q

What are some differences between eukaryote and prokaryote RNA?

A
  • Eukaryote RNA must get processed to get out of the nuclear pore
  • Eukaryote mRNAs separated from ribosomes by nuclear membranes
  • Prok ribosomes bind mRNA while RNA pol is still working.
67
Q

What is translated to a protein?

A

mRNA

68
Q

What carry out translation?

A

Ribosomes

69
Q

What is a codon?

A

a set of 3 nucleotides

70
Q

What does each codon indicate?

A

a specific amino acid that should be added to the protein

71
Q

What is the start codon what what does it tell the ribosome?

A

Start codon = AUG
It tells the ribosome where it should start adding amino acids

72
Q

What are the stop codons?

A

UAG, UAA, UGA

73
Q

Does the stop codon code for an amino acid?

A

no

74
Q

What is a ribosome?

A
  • a large structure composed of both protein and ribosomal RNA (rRNA)
75
Q

What is the function of a ribosome?

A

binds the messenger RNA and organizes translation

76
Q

What does tRNA do?

A
  • Delivers amino acids to ribosomes
  • binds to an amino acid on ones side
  • has an anticodon on the other side: a 3 nucleotide sequence that is complementary to the mRNA codon
77
Q

How are amino acids connected to the tRNA?

A
  • amnoacyl tRNA synthetase uses ATP energy to couple amino acids to the tRNA
  • The bond that hold the amino acid and the tRNA together is used as energy later to create the peptide bond in the growing protein chain
78
Q

What term reflects the energy of tRNAs coupled to amino acids?

A

charged

79
Q

What are the stages of Translation?

A
  • Initiation
  • Elongation 1
  • Elongation II
  • Elongation III
  • Termination
80
Q

What are the three binding sites in a ribosome for tRNA?

A

1) a (aminoacyl)
2) p (polypeptide)
3) e (exit)

81
Q

What occurs during translation initiation?

A
  • Ribosome attaches to mRNA
  • Ribosome moves down until it find the “START” codon (AUG)
  • The first tRNA binds to the “P”site of the ribosome
82
Q

What occurs during translation elongation I?

A
  • The tRNA that has the next correct anticodon can come into the “a” site.
  • From now on, all new tRNA enter “A” site
83
Q

What occurs during translation elongation II?

A
  • The amino acid on the “a” tRNA becomes linked to the polypeptide chain in the “P” position
  • the enzyme peptide transferase makes a peptide bond between the amino acids.
  • The polypeptide chain then disconnects from the “P” tRNA and is connected to the “A” tRNA
84
Q

What occurs during translation elongation III?

A
  • The ribosome moves down the mRNA
  • The tRNA with the polypeptide chain shits to the “P” position
  • The tRNA that unlinked its amino acid moves to the “E” (exit) site
85
Q

What occurs during translation termination?

A
  • a stop codon is encountered
  • stop codons do not bind tRNA molecules
  • stop codons attract proteins called release factors
    • fit in the “a” site
    • the polypeptide chain is cleaved off the tRNA in the “P” site.
  • Everything can be recycled for another round of translation
85
Q

What is a signal sequence?

A

n- terminus AA are signal for protein destination
often cleaved off after reaching destination

86
Q

What is the function of mRNA?

A

transcribes the genetic code from DNA into a form that can be read and used to make proteins

87
Q

What enzyme makes the peptide bond between amino acids in elongation II?

A

peptide transferase

Biology (6 decks)

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