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Amino Acids & Proteins Flashcards

1
Q

Structure of proteins influences…

A

The binding of different molecules

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2
Q

All peptides, polypeptides and proteins in the mammals are polymers of…

A

Alpha-L-amino acids

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3
Q

How many alpha-amino acids are used to make up proteins

A

20

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4
Q

Give the general structure of an amino acid

A
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5
Q

Which functional groups are found on alpha-amino acids, peptides and proteins?

A
  • Carboxylic (-COOH)
  • Amino (-NH2)

Attached to the same carbon atom (alpha carbon)

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6
Q

All amino acids in proteins exhibit which configuration?

Why?

A

Absolute steric configuration

Based on: Proteinogenic L-amino acids, related to L-glyceraldehyde

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7
Q

What is a monoamino monocarboxylic acid?

A

Amino acids with aliphatic R-groups

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8
Q

List the monoamino monocarboxylic acids

A
  • Glycine
  • Alanine
  • Valine
  • Leucine
  • Isoleucine
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9
Q

List the non-aromatic amino acids with Hydroxyl R-groups

A
  • Serine
  • Threonine
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10
Q

List the amino acids with sulphur-containing R-groups

A
  • Cysteine
  • Methionine
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11
Q

Give the amino acids with aromatic rings

A
  • Phenylalanine
  • Tyrosine
  • Tryptophan
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12
Q

Give the interaction

A

Hydrogen bond

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13
Q

Name the interaction

A

Van der Waals

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14
Q

Name the interaction

A

Disulphide bridge

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15
Q

Give the interaction

A

Ionic bond

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16
Q

What is happening in the figure?

A
  • Condensation of two amino acids
  • Forming a dipeptide with a peptide bond
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17
Q

What is shown?

What is shown in the red and blue circles?

A

Polypeptide chain

  • Red circle: N-terminal
  • Blue circle: C-terminal
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18
Q

Isoelectric point

A

pH value where the amino acid has no net charge

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19
Q

What classifies globular proteins?

A

They are water soluble

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20
Q

What classifies fibrous proteins?

A

They are water insoluble

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21
Q

What are intermediate proteins?

A
  • Water soluble
  • Rod-like
  • Found in myosin and fibrinogen
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22
Q

List the protein classifications differing by shape or water solubility

A
  • Globular proteins
  • Fibrous proteins
  • Intermediate proteins
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23
Q

List the proteins classifications by differing compositions

A
  • Simple proteins
  • Conjugated proteins
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24
Q

Simple proteins

A

During hydrolysis: Only amino acids/amino acid derivatives produced

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25
Conjugated proteins
Conjoined simple protein and non-protein compound
26
Prosthetic group of: Glycoproteins
Carbohydrates
27
Prosthetic group of: Nucleoproteins
Nucleic acids
28
Prosthetic group of: Phosphoproteins
Phosphoric acid
29
Prosthetic group of: Chromoproteins
Coloured prosthetic group
30
Example of a hemoprotein
Haemoglobin
31
Lipoproteins contain...
Lipid molecules
32
Prosthetic group of: Flavoproteins
Flavin
33
Prosthetic group of: Metalloproteins
Metals
34
List 3 conjugated protein types
* Glycoproteins * Nucleoproteins * Phosphoproteins
35
List protein types differing by function
* Contractile proteins * Transport proteins * Enzymes * Protein hormones * Toxic proteins
36
Primary structure of proteins
Amino acid sequence
37
Secondary structure of proteins
* α-helix/Beta-pleated sheet/Collagen helix * _Regularly repeating units_
38
Tertiary structure of proteins
* Polypeptide chain * 3-D structure by complete folding
39
Quarternary structure of proteins
Assembled subunits
40
In moist heat: Alpha-keratin →
Beta-keratin
41
Native conformation
* The 3-D conformation of a protein * Stable and active at optimal temp. and pH
42
Function of proteins arises from...
Chain-conformation | (Secondary & Tertiary structure)
43
Functional shape of a protein occurs during which stage?
Protein folding | (Active, native conformation formation)
44
Denaturation of proteins
Unfolding of chains | (Can be reversible - renaturation)
45
How does heat denature proteins? Examples
Breaks: * Hydrophobic interactions * Hydrogen bonds Examples: * Egg when it is fried * Skin when it is burned
46
How do acids and bases denature proteins?
By breaking ionic bonds
47
How do reducing/oxidising agents denature proteins?
Convert: Disulphide bonds → free sulfhydryl groups
48
How do hydrogen-bonding solvents denature proteins? Example
Disruption of hydrogen bonds Ethanol - precipitates bacteria proteins
49
How do heavy metal ions denature proteins? Example
React with _sulfhydryl bonds_ to form _carboxylate ions_ AgNO3 previously used to treat eyes of newborns for gonorrhoea
50
How does salting-out denature proteins? Example of use
Removes the hydrate hull Used in the separation of proteins
51
Denaturing agents used in gel electrophoresis
* Sodium dodecyl sulphate * Mercaptoethanol
52
Haemoglobin - Quarternary structure
53
Peptide bond: * Bond type * Location
* Primary, covalent bond * Between amino acids
54
Disulphide bond: * Bond type * Location * Example
* Primary, covalent bond * Between -SH containing side chains * 2 x Cysteine molecules form these bonds → Cystine formed
55
Ionic bond: * Bond type * Location
* Primary bond * Between polar, charged side chains * Between carboxyl group of an acidic and a basic amino group
56
Dipol-dipol interaction: * Bond type * Location
* Secondary bond * Between polar, non-charged sidechains ## Footnote *The partially negative portion of molecule attracted to partially positive portion of the other*
57
Van der Waals dispersion force: * Bond type * Location
* Secondary, hydrophobic bond * Between non-polar side chains * Weakest of all intermolecular forces* * Used when _numerous_ atoms are present* * A temporary* *partial negative charge on atoms*
58
List the _bonds_ of the secondary and tertiary structures
* Disulphide bond * Ionic bond * Dipol-dipol interaction * Van der Waals dispersion force * H-bonds
59
List the bonds of the quarternary structure
* Dispersion * Dipol * H-bond * Disulphide bond
60
Give examples of acidic amino acids
* Glu * Asp
61
Give examples of basic amino acids
* Lys * Arg * His

Biochemistry (21 decks)

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