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BIOL 130 > Module 5 > Flashcards

Module 5 Flashcards

1
Q

Amino Acid

A

The building blocks of proteins.

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2
Q

Primary Structure

A

The sequence of amino acids in a protein.

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3
Q

Alpha Helix

A

The polypeptide backbone is twisted in a right-hand coil stabilized by hydrogen bonds.

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4
Q

Tertiary Structure

A

The overall three-dimensional shape of a protein, formed by interactions between secondary structures. Becomes a protein.

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5
Q

Translation

A

Converting mRNA to a polypeptide chain.

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6
Q

Ribosomes

A

A complex structure of RNA and protein that synthesizes proteins from amino acids as directed by the sequence of mRNA.

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7
Q

Codon

A

A group of three adjacent nucleotides in mRNA that specifies an amino acid in a protein or that terminates protein synthesis.

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8
Q

Reading Frame

A

Following a start codon, a consecutive sequence of codons for amino acids.

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9
Q

Aminoacyl tRNA Synthetases

A

An enzyme that attaches a specific amino acid to a specific tRNA molecule.

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10
Q

Start Codon

A

AUG.

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11
Q

Initiation (Translation)

A

AUG codon is recognized and Met is established as the first amino acid in the new polypeptide chain.

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12
Q

Elongation (Translation)

A

Successive amino acids are added one by one to the growing chain.

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13
Q

Termination (Translation)

A

The addition of amino acids stops and the completed polypeptide chain is released from the ribosome.

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14
Q

Release Factor

A

A protein that causes a finished polypeptide chain to be freed from the ribosome.

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15
Q

Polycistronic mRNA

A

A single molecule of messenger RNA that is formed by the transcription of a group of functionally related genes located next to one another along bacterial DNA.

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16
Q

Post-Translational Modification

A

A modification that occurs after translation. It regulates the structure and function of proteins.

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17
Q

Signal-Recognition Particle (SRP)

A

An RNA-protein complex that binds with part of a polypeptide chain and marks the assembly for delivery to the endoplasmic reticulum (eukaryotes) or the cell membrane (prokaryotes).

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18
Q

Peptide Bond

A
  • CO - N
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19
Q

Secondary Structure

A

The level of protein structure resulting from regular and repeating hydrogen bonding interactions between atoms of the polypeptide backbone (α helix and β sheets).

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20
Q

Beta Sheet

A

The polypeptide chain folds back and forth on itself forming a pleated sheet stabilized by hydrogen bonds.

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21
Q

Quaternary Structure

A

The level of protein structure that results from the interactions of several different polypeptide chains (made up of different proteins).

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22
Q

mRNA

A

Messenger RNA.

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23
Q

A Site

A

Aminoacyl. The tRNA carrying the next amino acid binds.

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24
Q

P Site

A

Peptidyl. The tRNA carrying the polypeptide chain binds.

25
Q

E Site

A

Exit. The empty tRNA binds and leaves.

26
Q

Anticodon

A

The sequence of three nucleotides in a tRNA molecule that base pairs with the corresponding codon in an mRNA molecule.

27
Q

tRNA

A

Transfer RNA. Noncoding RNA that carries individual amino acids for use in translation.

28
Q

Genetic Code

A

The correspondence between codons and amino acids.

29
Q

Stop Codon

A

UAA, UAG, or UGA.

30
Q

Initiation Factors

A

A protein that binds to mRNA to initiate translation.

31
Q

Gene Regulation

A

The various ways in which cells control gene expression.

31
Q

Shine-Dalgarno Sequence

A

The initiation complex (initiation factors) is formed at one or more internal sequences present in the mRNA in prokaryotes.

32
Q

Protein Sorting/Protein Targeting

A

The process by which proteins end up where they need to be in the cell to perform their functions.

33
Q

Signal Sequences

A

An amino acid sequence in a protein that directs that protein to its proper cellular compartment.

34
Q

Glycine

A

R group is hydrogen so it is not asymmetric. Is small and increases the flexibility of the protein which can be important in the folding of the protein.

35
Q

Proline

A

R group is linked back to the amino group. It creates a kink or bend in the polypeptide chain and restricts rotation of the C-N bond, thereby imposing constraints on protein folding in its vicinity.

36
Q

Cysteine

A

The -SH groups of two cysteines can form an S-S disulfide bond which covalently joins the side chains.

37
Q

Disulfide Bonds (S-S)

A

Stronger than the ionic interactions of other pairs of amino acids and form cross-bridges that can connect different parts of the same protein or even different proteins.

38
Q

Denaturation

A

The process by which molecules are unfolded and therefore lose their structure and function.

39
Q

Chaperone Proteins

A

Help some proteins fold properly.

40
Q

Initiation Code

A

AUG (codes for Met).

41
Q

Elongation Factors

A

A protein that breaks the high-energy bonds of the molecule GTP to provide energy for ribosome movement and elongation of a growing polypeptide chain.

42
Q

Operon

A

A group of functionally related genes located in tandem along the DNA and transcribed as a single unit from one promoter in prokaryotes.

43
Q

Nuclear Localization Signals

A

A signal sequence that enables proteins to move through pores in the nuclear envelope.

44
Q

Signal-Anchor Sequence

A

In protein sorting, an amino acid sequence in a polypeptide chain that embeds the chain in the membrane.

45
Q

Protein Families

A

A group of proteins that are structurally and functionally related.

46
Q

Folding Domain

A

A region of a protein that folds in a similar way across a protein family relatively independently of the rest of the protein.

47
Q

Mutation

A

A change in the sequence of a gene.

48
Q

Natural Selection

A

Variations in genes that led to increase chance of survival and reproduction are passed down while others die off.

49
Q

Homodimer

A

A protein containing two identical subunits.

50
Q

Heterodimer

A

A protein containing two non-identical subunits.

51
Q

Uncharged

A

A tRNA without an amino acid attached.

52
Q

Charged

A

A tRNA with an amino acid attached.

53
Q

No Signal

A

Protein stays in cytosol.

54
Q

Amino Terminal Signal

A

On the end. Protein goes to chloroplast or mitochondria.

55
Q

Internal Signal

A

In the middle. Protein goes to the nucleus.

56
Q

N-Terminus

A

The free amino group that is at the amino end of the peptide.

57
Q

C-Terminus

A

The carboxyl group that is at the carboxyl end of the peptide.

58
Q

Peptide

A

Two amino acids bonded together.

BIOL 130 (11 decks)

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