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Pharmacy BSI > BSI Lecture 2 Protein Structure > Flashcards

BSI Lecture 2 Protein Structure Flashcards

1
Q

What are proteins made of ?

A

Amino acids

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2
Q

Primary protein structure

A

Amino acid sequence

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3
Q

Secondary protein structure

A

Formation of alpha helix and beta sheets

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4
Q

Tertiary protein structure

A

Overall 3-dimensional shape of protein

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5
Q

Quaternary protein structure

A

More than one polypeptide (dimers, oligomers)

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6
Q

How many amino acids are there?

A

20 (8 essential and 12 nonessential)

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7
Q

What is the basic structure of an amino acid?

A

Central carbon (alpha carbon) with a single hydrogen atom, amino group, a carboxyl group, and a side chain (R group).

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8
Q

Asp

A

Aspartic acid, negative (acidic side chain)

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9
Q

Glu

A

Glutamic acid, negative (acidic side chain)

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10
Q

Arg

A

Arginine, positive (basic side chain)

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11
Q

Lys

A

Lysine, positive (basic side chain)

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12
Q

His

A

Histidine, positive (basic side chain)

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13
Q

Asn

A

Asparagine, uncharged polar

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14
Q

Gln

A

Glutamine, uncharged polar

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15
Q

Ser

A

Serine, uncharged polar

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16
Q

Thr

A

Threonine, uncharged polar

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17
Q

Tyr

A

Tyrosine, uncharged polar

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18
Q

Ala

A

Alanine, nonpolar

19
Q

Gly

A

Glycine, nonpolar

20
Q

Val

A

Valine, nonpolar

21
Q

Leu

A

Leucine, nonpolar

22
Q

Ile

A

Isoleucine, nonpolar

23
Q

Pro

A

Proline, nonpolar

24
Q

Phe

A

Phenylalanine, nonpolar

25
Q

Met

A

Methionine, nonpolar

26
Q

Trp

A

Tryptophan, nonpolar

27
Q

Cys

A

Cysteine, nonpolar

28
Q

Which amino acids can be phosphorylated? Why?

A

Serine, Threonine, and Tyrosine because they have a hydroxyl group (OH).

29
Q

Which amino acid can form disulfide bonds? Why?

A

Cysteine because it contains SH functional group

30
Q

What are the 8 essential amino acids that can’t be produced by the body?

A

Threonine, Methionine, Lysine, Valine, Leucine, Isoleucine, Phenylalanine, Tryptophan

31
Q

3 Facts about Primary Structures

A
  1. Stabilized by peptide bond
  2. Peptide bond is covalent
  3. Bond forms between amino group and and carboxyl group, resulting in the loss of a water molecule
32
Q

What is the end of the protein?

A

Carboxyl Group

33
Q

What is the beginning of the protein?

A

Amino Group

34
Q

4 Facts about Secondary Structures

A
  1. Alpha helix and beta sheets are most common
  2. Hydrogen bonds stabilize
  3. Hydrogen bonds are non-covalent
  4. Hydrogen bond between back
  5. Very stable and rigid structures
  6. These structures do not involve unique side chains, therefore they do not require a unique amino acid sequence to form
35
Q

4 Facts about Tertiary Structures

A
  1. Folded polypeptide strand into three dimensional shape (no two proteins will have the same tertiary structure)
  2. Determined by unique amino acid sequence
  3. Domains
  4. Types of bonds that will stabilize tertiary structures are Hydrogen bonds, Ionic bonds, hydrophobic interactions, Van der Waals attractions, and Disulfide bonds
36
Q

Facts about Quaternary structures

A

More than one polypeptide chain (dimers and oligomers)

37
Q

Hydrogen bond

A

weak interactions that form between a hydrogen with a partial positive charge and a more electronegative atom

38
Q

Hydrophobic interaction

A

The tendency of nonpolar molecules in a polar solvent (usually water) to interact with one another.

39
Q

Ionic bond

A

The complete transfer of valence electron(s) between atoms that form a cation and anion.

40
Q

Van der Waals attraction

A

The attraction of intermolecular forces between molecules.

41
Q

Disulfide bridge

A

A covalent bond derived from two thiol groups.

42
Q

Homodimer

A

Formed by two identical molecules (a process called homodimerisation)

43
Q

Heterodimer

A

A heterodimer is formed by two different macromolecules (called heterodimerisation).

44
Q

Oligomer

A

a molecular complex that consists of a few monomer units.

Pharmacy BSI (58 decks)

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