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Amino Acids and Proteins, Slides of Chemistry

A comprehensive overview of amino acids and proteins, covering topics such as protein function, the structure and properties of amino acids, the formation of peptide bonds, and the different levels of protein structure (primary, secondary, tertiary, and quaternary). It also discusses protein denaturation, the importance of amino acid sequences in determining protein function, and methods for protein separation and purification. The detailed information on the various aspects of amino acids and proteins makes this document a valuable resource for students and researchers in fields related to biochemistry, molecular biology, and biotechnology.

Typology: Slides

2023/2024

Available from 08/05/2024

kaa-elka
kaa-elka 🇮🇩

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AMINO ACIDS AND
PROTEINS
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AMINO ACIDS AND

PROTEINS

PROTEIN FUCTION

Catalyst  enzyme

Transport  blood, membrane protein

Nutrient  seed protein, ovalbumin, casein

Skeletons  collagen, keratin, fibroin

Defense  immunoglobulin, fibrinogen,

thrombin

Regulator  hormone

Protein is a polymer of “amino acid”

monomers

AMINO ACIDS IN SOLUTION

H

NH

2

COOH
C
R
H

NH

3

COO
C
R

Un-ionized Zwitterion (ion dipolar)

H

NH

2

COOH
C
R
H

NH

2

COOH
C
H

Glisin

AMINO ACIDS AT VARIOUS pH

H

NH

2

COO
C
R
H

NH

3

COO
C
R
H

NH

3

COOH
C
R

pH = 1 pH = 7 pH = 11

AMINO ACID

The R group of each amino acid is different

Structure

Size

Charge

Solubility

Amino acid groups:

Non-polar aliphatic R groups

Aromatic R groups

Polar un-charged R groups

Negatively charged R groups

Positively charged R groups

AMINO ACID “R” GROUP

CYSTINE

AMINO ACID

Examples of non-standard amino acids

  • 4-hydroxyproline  plant cell walls
  • 5-hydroxylysine  collagen
  • N-methyllisine  myosin
  • γ-carboxyglutamate  prothrombin
  • Selenocysteine  glutathione

peroxidase

  • Ornithine, citrulline in watermelon

AMINO ACID

Each amino acid has a specific titration curve

Each amino acid has different acid and base

properties.

TITRATION CURVE

Titration curve of 0.1 M Alanine

NINHYDRIN REACTION

PEPTIDE BONDS

PEPTIDE BONDS (cont.)

Two amino acids  dipeptide

Three amino acids  tripeptide

Several amino acids  oligopeptide

Many amino acids  polypeptide

(MW < 10,000)

Read from left (N-terminal) to right (C-terminal)

Peptide bonds are very stable  hydrolysis of

peptide bonds  exergonic reaction

Disulfide bonds are also very important especially

those that function extracellularly

Eg: insulin and immunoglobulin

PEPTIDE

Terminal amino residues

H

H

3

N C C

R

1

O H

N C C

R

2

O H

N C C

R

3

O H

N C C

R

4

O H

N C C

R

5

O

O

Terminal carboxyl residue

Pentapeptide

= R

= R