Amino acids

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54 Terms

1
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What is an amino acid theorized to have been created from?

Nature acting on atmospheric gases

2
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What do amino acids link together to form?

Polypeptides (≤50) and proteins (≥50)

3
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What functional groups do amino acids possess?

An amine group (basic) and a carboxylic acid group (acidic)

4
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How many amino acids are used in protein synthesis?

20 (known as the "magic 20")

5
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Why are they called α-amino acids?

Both the amine and acid group are attached to the α-carbon

6
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What is attached to the α-carbon in an amino acid?

A hydrogen atom and a unique R-group

7
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What determines the unique identity of an amino acid?

The R-group

8
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How are amino acids best classified?

According to the nature of their R-group side chain

9
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What are the four R-group classifications?

Non-polar, polar, acidic, basic

10
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What functional groups are most distinguishing in amino acids?

α-amino and α-carboxylic acid groups

11
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What is a zwitterion?

A charged amino acid that simultaneously exists as both a cation and anion

12
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Why are amino acids water soluble?

Because they are charged (zwitterions)

13
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What does it mean for an amino acid to be amphoteric?

They can act as both an acid and a base

14
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How do amino acids behave in acidic solutions?

They are positively charged

15
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How do amino acids behave in basic solutions?

They are negatively charged

16
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Why are amino acids considered pseudo-buffers?

They resist dramatic pH changes due to their amphoteric nature

17
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What role do amino acids play in the body?

They help regulate pH

18
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What forms when amino acids link together?

Polypeptides and proteins

19
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When is a chain officially designated a protein?

When it contains 50 or more amino acids

20
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What are the size ranges of proteins?

From 35,000 g/mol to 55,000,000 g/mol

21
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What are fibrous proteins?

Proteins that give structure to organs, skin, muscle, tendons, and bone

22
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What are globular proteins?

Proteins that act as transporters and biological catalysts (enzymes)

23
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What determines a protein's function?

Its structure

24
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What are the four levels of protein structure?

Primary, secondary, tertiary, quaternary

25
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What is the primary structure of a protein?

The sequence of amino acids

26
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What is another name for primary structure?

Foundational structure

27
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How is primary structure visually represented?

A string of beads (each bead = amino acid)

28
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Which groups are typically placed at the start and end of the sequence?

Amine group at start, acid group at end

29
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What is a disulfide bridge?

A covalent bond between sulfurs from different cysteine amino acids

30
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What was the first protein structure discovered?

Bovine insulin by Frederick Sanger in 1953

31
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What forms secondary structure?

Hydrogen bonding

32
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What are two common types of secondary structure?

Pleated sheet and β-helix

33
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What causes tertiary structure?

Combination of all bonding and interactions between side chains

34
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What forces influence tertiary structure?

Hydrogen bonding, electrostatic interactions, disulfide bridges, hydrophobic and hydrophilic interactions

35
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Where do non-polar side chains go in tertiary structure?

To the protein's interior

36
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Where do polar and ionic side chains go?

On the outside in aqueous environments

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What causes protein folding and contortion?

Aqueous environment trying to hide non-polar parts

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What is quaternary structure?

Interaction between two or more protein chains (subunits)

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What are the protein chains in quaternary structure called?

Subunits

40
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What is hemoglobin an example of?

Quaternary protein structure

41
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How many protein chains does hemoglobin have?

Four: 2 α-chains (141 AA’s) and 2 β-chains (146 AA’s)

42
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What does each hemoglobin chain contain?

One heme molecule

43
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What does heme do?

Binds iron to histidine and oxygen simultaneously

44
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What is hemoglobin's role?

Carries oxygen to cells and CO2 back to lungs

45
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How is myoglobin different from hemoglobin?

One protein strand (153 AA’s) and one heme; has only tertiary structure

46
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What is denaturation?

Loss of all protein structure except primary

47
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What causes denaturation?

Extreme heat, high acid or base

48
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What happens to protein function after denaturation?

It is destroyed

49
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What is an everyday example of denaturation?

Frying an egg

50
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What is putrefaction?

Post-mortem protein, nucleic acid, carbohydrate, and lipid breakdown

51
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What are fibrous proteins made of?

Repeating amino acid units

52
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What makes fibrous proteins stable?

More cross-linking and hydrophobic side chain aggregation

53
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Why are fibrous proteins less water soluble?

Hydrophobic side chains protrude from the molecule

54
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How long do fibrous proteins persist after death?

Several months