2.4 - Quaternary Structure Flashcards

1
Q

non-bonded interactions (4)

A
  1. electrostatic interactions
  2. hydrogen bonds
  3. hydrophobic interactions
  4. van der waals forces
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2
Q

acid dissociation constant

A

pH at which charged amino acids carry no net charge

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3
Q

+ve charged R group amino acids (3)

A
  1. lysine (Lys, K)
  2. arginine (Arg, R)
  3. Histidine (His, H)
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4
Q

what affects basic and acidic amino acid R groups?

A

pH of the environment

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5
Q

-ve charged R group amino acids (2)

A
  1. glutamic acid (Glu, E)
  2. aspartic acid (Asp, D)
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6
Q

when do salt bridges form?

A

at neutral pH, when most charged side chain R groups are ionised

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7
Q

how do salt bridges form?

A

electrostatic interaction occurs between a +ve and -ve side chain (if they are closely arranged in space)

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8
Q

effect of salt bridge formation

A

charge spread across whole residue

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9
Q

where do H-bonds form between amino acids?

A

between R groups (as well as main chain)

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10
Q

hydrophobic effect

A

apolar (non-polar) molecules aggregate in presence of water

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11
Q

where are hydrophobic residues usually found in molecule?

A

in the centre of the folded molecule

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12
Q

van der waals

A

weak electrostatic interaction between atoms in close proximity, generated by dipoles from the electron cloud

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13
Q

why cant atoms interacting via van der waals come too close?

A

-vely charged e- will repel (van der waals radius)

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14
Q

multimeric protein nomenclature: identical chains

A

homo-

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15
Q

multimeric protein nomenclature: different chains

A

hetero-

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16
Q

multimeric protein nomenclature: 2 chains

A

dimer

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17
Q

multimeric protein nomenclature: 3 chains

18
Q

multimeric protein nomenclature: 4 chains

19
Q

fibrous proteins

A

elongated and structural role in nature - provide support, shape or protection

20
Q

examples of fibrous proteins (3)

A
  1. collagen
  2. keratin
  3. silk
21
Q

collagen role

A

connective tissue

22
Q

examples of collagen (4)

A
  1. tendons
  2. cartilage
  3. organic matrix of bone
  4. cornea
23
Q

collagen structure

A

3 intertwined polypeptide chains that form triple helix

24
Q

how many distinct versions of collagen do humans have?

A

16 - differ in primary sequence

25
globular protein structure (2)
1. spherical shape 2. exist in enormous variety of 3D structures
26
globular protein frequency vs fibrous proteins
globular much more numerous
27
classifications of protein interactions (2)
1. permanent 2. transient
28
characteristics of permanent protein interactions
tight binding with strong affinities
29
characteristics of transient protein interactions
weaker and more dynamic
30
characteristics of protein-protein interaction sites (5)
1. hydrophobic 2. surface accesible 3. protruding 4. planar 5. specific residue propensities
31
membrane proteins
interact with lipids and have very specific primary sequences and structures
32
what is gramicidin A
antibiotic peptide
33
where is gramicidin found?
DMPC lipid bilayer and water
34
gramicidin A action (2)
1. forms pore in cell wall of bacteria letting out monovalent cations (K+/Na+) 2. membrane potential disappears and bacteria dies
35
gramicidin structure (2)
1. 15 amino acids 2. helical
36
how does gramicidin form a channel
head-to-head dimer
37
types of ion channels (4)
1. simple pores 2. substrate gated channels 3. voltage-gated channels 4. pumps
38
example of simple pore ion channels
GAP junctions
39
example of substrate gated ion channel
nicotinic receptor
40
example of voltage-gated ion channel
K+ channel
41
examples of pump ion channels (2)
1. ATP-synthase 2. K+/Na+-ATPase
42
requirements for drug to interact with protein to inhibit/enhance function (3)
1. correct size 2. right chemical properties to fit active site 3. compete with substrate