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BC3001: Structural & Experimental Biochemistry > Protein Structure & Function > Flashcards

Protein Structure & Function Flashcards

1
Q

What type of reaction creates peptide bonds? And where does it occur?

A

Condensation reaction between the carboxylic and amino group

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2
Q

Which amino acid is the most HYDROPHOBIC?

A

Isoleucine

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3
Q

Which amino acid is the most HYDROPHILIC?

A

Arginine

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4
Q

What does a POSITIVE value indicate on a hydropathy index?

A

A polypeptide most likely to be found in the membrane

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5
Q

TRUE OR FALSE?
Polypeptide chains are planar?

A

True

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6
Q

TRUE OR FALSE?
Alpha helices have one positive angle and one negative angle?

A

False.
They have 2 negative angles

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7
Q

TRUE OR FALSE?
Beta pleated sheets have one positive angle and one negative angle?

A

True

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8
Q

Which amino acids do Zinc Finger Motifs require?

A

2x Cysteine
2x Histidine

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9
Q

What amino acids are required for catalytic sites on enzymes?

A
  • Serine
  • Asparagine
  • Histidine
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10
Q

What interactions contribute to the stabilisation of the protein molecule?

A
  • Hydrophobic Ionic Interactions
  • Hydrogen bonding
  • Van der Waals forces
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11
Q

What function(s) does Phosphorylation usually modulate?

A

Regulation

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12
Q

What function(s) does Glycosylation usually modulate?

A
  • Folding
  • Stability
  • Regulation
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13
Q

What function(s) does Acetylation usually modulate?

A

Regulation

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14
Q

Which amino acids have a phosphate group added to them during Phosphorylation?

A
  • Serine
  • Threonine
  • Tyrosine
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15
Q

What function(s) does Hydroxylation usually modulate?

A

Regulation

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16
Q

What function(s) does Methylation usually modulate?

A
  • Regulation - epigenetics
17
Q

Which amino acids are involved in Hydroxylation?

A
  • Lysine
  • Asparagine
18
Q

TRUE OR FALSE?
Every AA residue is essential for function?

A

False.
Every AA contributes towards the final structure, every residue is NOT essential for function

19
Q

What percentage of human proteins are polymorphic?

A

20-30%

20
Q

Where do cells acquire the molecules and ions they need?

A

Extracellular Fluid (ECF)

21
Q

What is a Chemical Gradient?

A

A difference in solute concentrations across a membrane

22
Q

What is an Electrical Gradient?

A

A difference in potential/charge across a membrane

23
Q

What is Resting Potential?

A

Static membrane potential

24
Q

What is an Action Potential?

A

Rapid rise and fall in membrane potential causing similar cells to depolarise

25
Q

What ions flow in and out of a cell during an Action Potential?

A
  • INWARDS - Na+
  • OUTWARDS - K+
26
Q

What AA sequence is found in the signature motif of K+ channels?

A
  • Threonine
  • Valine
  • Glycine
  • Tyrosine
  • Glycine
27
Q

Which technique was mostly used for Ion Conductance measurements?

A

Patch Clamping - single channel recordings

28
Q

What shape is the Bacterial KcsA Channel?

A

V shaped tetramer

29
Q

How many residues does the Bacterial Kcs Channel have?

A

158

30
Q

How many subunits does the Bacterial Kcs Channel have?

A

Four identical subunits

31
Q

What is in the middle of the membrane of the the Bacterial Kcs Channel?

A

Hydrated K+

32
Q

What THREE segments make up the subunit structure of the Bacterial Kcs Channel?

A
  1. Selectivity Filter
  2. Cavity / Lake
  3. Internal Pore
33
Q

What amino acids make up the Selectivity Filter for K+ channels?

A

TVGYG
* Four layers of carbonyl atoms (VGYG)
* One layer of hydroxyl atoms (Thr)

34
Q

How many binding sites does the Selectivity Filter have for dehydrated K+?

A

4

35
Q

How many coordination sites do K+ ions have?

A

8 sites occupied by H20 molecules

36
Q

Which negatively charged amino acids are at the K+ ion channel entrance?

A

Glu and Asp

37
Q

What amino acids are on each voltage sensor of the ion channel?

A

4 Arg

38
Q

How does ion channel inactivation occur?

A

N-terminal ball plugs the pore from the cytoplasmic side

BC3001: Structural & Experimental Biochemistry (13 decks)

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