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BIOC practice Q's > Tutorial 1 proteins lecture 3 - 6 > Flashcards

Tutorial 1 proteins lecture 3 - 6 Flashcards

1
Q

what are the common functions of proteins?

A
  • catalyze reactions
  • structure - collagen
  • transport molecules - hemoglobin and myoglobin
  • immune protection - antibodies
  • replicate dna / rna - polymerase
  • cell signal - insulin
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2
Q

label each circled part of amino acid

A

H2N - amino group

R - sidechain

COOH - carboxyl group

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3
Q

non polar uncharged
amino acid
Alanine

A

COO-
CH
H3N+
CH3

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4
Q

polar uncharged
amino acid
Asparagine

A 
COO-
CH
H3N+
CH2
C
H2N
O
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5
Q

polar uncharged
amino acid
Serine

A 
COO-
CH
H3N+
CH2
OH
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6
Q

polar -‘ve charge
amino acid
Glutamic acid

A 
COO-
CH
H3N+
CH2
CH2
COO-
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7
Q

define each of the levels of protein structure

A 
primary
secondary
super-secondary
domain
tertiary
quaternary
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8
Q

define primary protein structure

A

amino acid sequence

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9
Q

define secondary protein structure

A

3D arrangement of a protein chain over a short region.

a-helices, b sheets / strands

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10
Q

define super-secondary protein structure

A

groups of secondary structures

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11
Q

define domain protein structure

A

super-secondary structure with a specific function

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12
Q

define tertiary protein structure

A

3D structure of a complete protein chain

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13
Q

define quaternary protein structure

A

interchain packing and structure for a protein that contains multiple protein chains

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14
Q

what type of bonds stabilise primary structure?

A

Peptide bond - covalent

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15
Q

what type of bonds stabilise secondary structure?

A

hydrogen bonding stabilises a-helices & b-structure

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16
Q

what types of bonds stabilise tertiary structure?

A

hydrogen bonding,
hydrophobic interactions,
disulfide bridges (covalent),
salt bridges / ionic bonds

17
Q

what types of bonds stabilise quaternary structure?

A

same as tertiary

hydrogen bonding,
hydrophobic interactions,
disulfide bridges (covalent),
salt bridges / ionic bonds

18
Q

describe the difference between a parallel and an antiparallel beta sheet

A

parallel

  • 2 strands running in same direction (N - C)
  • H bonds in zig zag

antiparallel

  • 2 strands run in opposite direction (N - C)
  • H bonds vertical
19
Q

describe the properties of glycine and proline that make them suitable for turns, but unfavoured in alpha helices

A

helix breakers

small side chains make glycine very flexible. decrease steric hinderance.

proline is rigid, built in turn because of the bonding between the R group and the amino group.

20
Q

describe in general terms , the process by which an unfolded polypeptide chain, folds into its native (normal) conformation (shape)

A
  • formation of short 2° structure segments
  • nucleic come together growing cooperatively to form a domain
  • domains come together (but 3° structure still partly disordered
  • small conformational adjustments to give compact native structure
21
Q

what are the bonds that are broken when a protein becomes unfolded?

A

all except covalent bonds

  • H bonds
  • ionic interactions
  • hydrophobic interactions
22
Q

what effect does unfolded protein have on the function?

A

destroys function
unfolded no longer has the 3D shape to carry out function

the function is determined by shape

23
Q

with an example describe how misfolding of a proteincan lead to a disease

A

cystic fibrosis

prion diseases - 1 misfold prion introduce to system and cause other proteins to misfold. this results in proteins aggregating together forming amyloid plaque eg kuru, mad cow (BSC). physically ingested.

alzheimers disease - misfold proteins aggregate to form plaque

24
Q

what is a post-translational modification (PTM)

A

a chemical group that is added to an amino acid residue after translation has occurred

chemical groups are added covalently

eg phosphorylation, glycosylation, methylation, lipidation, acetylation

25
Q

what is phosphorylation?

A

the addition of a phosphate group to an amino acid

26
Q

how (in structure-function terms) does phosphorylation affect protein function?

A

activate / deactivate proteins

adds large -‘ve charge can cause conformational change within protein that will affect function of protein

BIOC practice Q's (8 decks)

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