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BIOL 130 > Module 5 (Protein Structure, Function and Synthesis) > Flashcards

Module 5 (Protein Structure, Function and Synthesis) Flashcards

1
Q

N-Terminus

A

The end of an amino acid chain that has the amino group

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2
Q

C-Terminus

A

The end of an amino acid chain that has a carboxyl group

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3
Q

mRNA

A

Messenger RNA

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4
Q

tRNA

A

Transfer RNA

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5
Q

What’s the difference between Basic and Acidic amino acids?

A

Basic: has amine group (usually + charge)
Acidic: has carboxylic acid in the side chain (usually - charge)

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6
Q

Hydrophobic Amino Acids

A

Hydrophobic R groups, weak van der Waals forces

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7
Q

Hydrophilic Amino Acids

A

Contain electronegative elements (N or O), unequal charge -> R group interact with each other or H bonding
Typically found on the “outer” surface of proteins

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8
Q

Why is Glycine a special amino acid?

A

R group is Hydrogen, small and nonpolar, increases flexibility of the polypeptide backbone

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9
Q

Why is Proline a special amino acid?

A

R group links back to the amino group, restricts rotation of the C-N bond, limits the protein folding around proline

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10
Q

Cysteine

A

R group contains a -SH group, two cysteines can form a disulfide bond (cross bridge, which can connect different parts of the same protein or different proteins together)

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11
Q

Levels of Protein structure

A

Primary, Secondary (2°), Tertiary(3°), Quaternary (4°)

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12
Q

Primary Structure

A

Linear sequence of amino acids that make up a polypeptide chain
- Amino to carboxyl (N-terminus to C-terminus)
- R-groups alternate position of either side of the amino acid chain

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13
Q

Secondary Structure

A

Conformation of portions of the polypeptide chain (alpha helix and beta sheet)

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14
Q

Alpha Helix

A
  • Very stable
  • Right-hand helices
  • Formed from H-bonds to the 4th amino acid neighbour (functional groups)
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15
Q

Beta Sheet

A
  • Pleated formation
  • Can be parallel and antiparallel
  • Stabilized by H-bonds (functional groups)
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16
Q

Tertiary Structure

A
  • Conformation of the entire protein
  • How regions of 2° conformations are oriented
  • Functional form
  • Determined by R-group interactions
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17
Q

R-group Interactions

A
  • Spatial distribution of the hydrophilic and hydrophobic R groups
  • Chemical bonds and interactions that form between the R groups (include hydrogen bonds, hydrophobic bonds, ionic bonds, disulfide bonds)
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18
Q

Disulfide bonds

A

Covalent bond between two cysteine residues

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19
Q

Quaternary Structure

A

The arrangement of multiple subunits of polypeptides, also R-group interactions

20
Q

Homodimer

A

Protein containing two identical subunits

21
Q

Heterodimer

A

Protein containing two non-identical subunits

22
Q

Components of Translation

A

mRNA, Ribosome, tRNAs, Aminoacyl tRNA synthetases, Initiation factors, elongation factors and release factors

23
Q

Ribosomes

A

Location of translation, protein factories, small subunit and large subunit
- Reads mRNA 5’-3’

24
Q

Codon

A

Three adjacent nucleotides, specifies the placement of an amino acid

25
Q

Methionine

A

Start codon of AUG

26
Q

A-site

A

Site in ribosome where aminoacyl tRNA is accepted

27
Q

P-site

A

Site of peptide bond formation

28
Q

E-site

A

Where tRNA exits the ribosome

29
Q

tRNA composition

A

Composed of 70-90 nucleotides
- 3’ hydroxyl site (where the specific amino acid attaches)
- Anticodon loop

30
Q

Aminoacyl tRNA synthestases

A

Enzymes that connects specific tRNA to specific amino acids
(VERY ACCURATE)

31
Q

Uncharged tRNA

A

tRNA without an amino acid attached

32
Q

Charged tRNA

A

tRNA with an amino acid attached

33
Q

How many codons are there?

A

64 codons, codes for 20 amino acids

34
Q

Initiation in Translation

A

Binds to initiation complex. Small subunit of ribosome scans for start codon, AUG codon is recognized and Met is the first amino acid, large subunit binds to small subunit

35
Q

Elongation in Translation

A

Each amino acid is added to the polypeptide chain, previous tRNA moves into P-site, new tRNA in A-site, peptide bond forms, ribosome shifts one codon, opening up A-site

36
Q

Termination in Translation

A

A stop codon is reached (UAA, UAG, UGA) and a release factor binds to the A site

37
Q

Prokaryotic Initiation Complex

A

Initiation complex is formed at one or more internal sequences in mRNA
- Shine-Dalgarno sequence

38
Q

Eukaryotic Initiation Complex

A

Formed at 5’ cap

39
Q

Posttranslational modification

A

An inactive protein must be activated by cleavage or other types of posttranslational modification

40
Q

Protein Sorting

A

Specific signal sequences determine what happens to a protein after translation

41
Q

No signal sequence

Protein Sorting

A

Protein stays in cytosol

42
Q

Amino terminal signal

Protein Sorting

A

Protein goes to chloroplast or mitochondria

43
Q

Internal signal

Protein Sorting

A

Protein goes to the nucleus

44
Q

Signal recognition particle (SRP)

A

Recognizes specific amino terminal sequence that codes for transport to the ER

45
Q

Proteins produced by ribosomes on the rough ER could be found

A
  • Embedded in the ER membrane (inserted as it is synthesized)
  • Within the lumen of the endomembrane system
  • Secreted out of the cell

BIOL 130 (10 decks)

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