Drug Bonds Flashcards

1
Q

What is the primary structure of a protein?

A

Linear sequence of amino acids

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2
Q

What characterizes the secondary structure of a protein?

A

Folding of amino acid chain into regular patterns

E.g. alpha helices and beta sheets

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3
Q

Define tertiary structure in protein.

A

Folding of protein into overall 3D structure

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4
Q

What is the quaternary structure of a protein?

A

Assembly of subunits to form functional protein

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5
Q

What are the two termini of an amino acid?

A
  • α N terminus * C terminus
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6
Q

What is a binding domain?

A

A region that interacts specifically with another molecule

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7
Q

What is a pharmacophore?

A

Minimum set of structural features a molecule must have to fit into a target’s binding domain

The part of a molecule responsible for its biological activity

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8
Q

What is the bond strength range for covalent bonds?

A

200-800 kJ/mol

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9
Q

What is the bond strength range for ionic bonds?

A

40-200 kJ/mol

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10
Q

True or False: Hydrogen bonds are the strongest type of bond.

A

False

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11
Q

What is the typical strength range for hydrogen bonds?

A

2-30 kJ/mol

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12
Q

What is required for hydrogen bonds to form?

A
  • Electronegative atom with lone pair(s) * Electronegative atom covalently bonded to hydrogen
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13
Q

Fill in the blank: Covalent bonds involve _______.

A

Electron sharing

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14
Q

What are hydrophobic bonds?

A

Interactions between nonpolar molecules in aqueous environments

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15
Q

What is the significance of gain in entropy (ΔS)?

A

Indicates the spontaneity of a reaction

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16
Q

What is the strength range of Van der Waals forces?

A

0.4-4 kJ/mol

17
Q

What type of bonds are stronger than hydrogen bonds?

A

Ionic bonds

18
Q

Define anion.

A

An atom that has gained an electron

19
Q

Define cation.

A

An atom that has lost an electron

20
Q

What is the role of valence shell electrons?

A

Involved in forming bonds between atoms

21
Q

What are the properties of hydrogen bonds?

A

Highly directional and moderately strong

Atoms have to be in a straight line for the bond to have full strength

22
Q

What is the definition of electronegativity?

A

The tendency of an atom to attract electrons

23
Q

What is a good hydrogen bond donor?

A

An electronegative atom covalently bonded to hydrogen

24
Q

What is a good hydrogen bond acceptor?

A

An electronegative atom with lone pairs

25
True or False: Hydrogen bonds can only be donors.
False
26
What are the positively charged amino acids?
Arginine (Arg/R) Histidine (His/H) Lysine (Lys/K)
27
What are the negatively charged amino acids?
Aspartic acid (Asp/D) Glutamic acid (Glu/E)
28
What are the polar uncharged amino acids?
Serine (Ser/S) Threonine (Thr/T) Asparagine (Asn/N) Glutamine (Gln/Q)
29
What are the hydrophobic amino acids?
Alanine (Ala/A) Valine (Val/V) Isoleucine (Ile/I) Leucine (Leu/L) Methionine (Met/M)
30
What are the hydrophilic amino acids?
Phenylalanine (Phe/F) Tyrosine (Tyr/Y) Tryptophan (Trp/W)
31
What are the special cases in amino acids?
Glycine (Gly/G) Proline (Pro/P) Cysteine (Cys/C) Selenocysteine (Sec/U) = less commonly found
32
What are covalent bonds?
Share electrons
33
What is an important feature of cations?
Can also do cation-Pi interactions where the positive charge interacts with electron clouds of aromatic rings in amino acids This is important in binding ACh to nicotine receptors
34
Order of electronegativity
O > N > S = C > H
35
Van der Waals forces
Strongly dependent on distance —> too close = repel and too far = little interaction Permanent dipoles - instantaneous dipoles = due to random fluctuations in the electron field results in uneven distribution of electrons - induced dipoles = neighbouring molecule causes partial charges Very weak