Biochem Lec Lesson 1 Groups of amino acids according to polarity (ability to

bond with water) of side chains:

AMINO ACIDS AND PROTEINS
Protein 1.Hydrophobic Amino Acids
- from the Greek Word “proteios” (of Importance) - Non polar
-Naturally occurring polymer in which the monomer - Contact with another
units are amino acids. - Found in the interior of proteins & isolated from
water
Cellular Functions of Proteins: 9 Amino Acids:
Enzymes  Alanine
- Are proteins by nature  Valine
- Biological catalyst  Leucine
- Hasten reaction  Isoleucine
Ex: amylase – hasten the digestion of starch  Glycine – simplest amino acid
Pepsin – catalyze the breakdown of proteins  Phenylalanine
Trypsin –  Proline – not an alpha amino acid
Lipase – enzyme that digest fats  Tryptophan
 Methionine
Antibodies
- Aka immunoglobulins (immuno= function for 2. Hydrophilic amino acids
the immune system) - Attracted to polar water molecules; often found
- Specific protein molecules produced by on surface of proteins
specialized cells of immune system (Plasma 3 classes:
Cells= different forms of lymphocytes; from B a. Polar, Neutral Amino Acids
lymphocytes) in response to foreign bodies - Have R groups that have high affinity to water
(antigens) - Not ionic at pH 7
- Bodies are always hostile to anything foreign
 Serine
Transport Proteins  Threonine
- Carry materials from one place to another  Tyrosine
Ex: transferrin – protein that transports iron  Cysteine
Hemoglobin – protein that transports oxygen  Asparagine
Myoglobin – protein that carries oxygen to muscles  Glutamine

Regular Proteins b. Negatively charged Amino Acids

- Control many aspects all function including - Have ionized carboxyl group in their side chains
metabolism and reproduction - At pH 7, these amino acids have net charge
- Hormones (chemical messengers) instruction of -1.
from brain - They are acidic in ionization if the carboxylic
acid releases a proton
Structural Proteins - Negatively charged even at pH 7
- Provides mechanical support to large animals  Glutamate – glutamic Acid
and provide coverings  Aspartase – aspartic acid
- Ex: Keratin (collagen)
c. Polar positively charged amino acid
Movement Proteins - At PH 7, have a net positive charge because of
- Necessary for all forms of movement their

Nutrient Proteins
- Sources of amino acid for embryos or infants  Lysine
Ex: Albumin (egg), Casein (Milk)  Arginine
 Histidine
Alpha- amino Acids
- Building blocks of protein THE PEPTIDE BONDS
- Amino froup (NH2) attached to the C atom - Amide group that links amino acids
Dipeptide bond – the molecule formed by condensing
H2N (non-ionized) H3N (ionized) Carboxyl = COOH or two amino acids.
COO
  N-terminal amino acid- with free NH3
 C-terminal amino acid with a free COOH group
Condensation Reaction – diffusion of 2 amino acids
(dehydration = removal of two H)

Nomenclature:
Peptides- named as derivatives of C- terminal amino
acid, which receives its

ine -> iyl

-yl suffix replaces the –ine or –ic acid ending of the AA
name.

> tryptophan (tryptophyl)

> cysteine (cysteinyl)
> glutamine (glutamyl)
> asparagine (asparaginyl)

*glutamic acid = glutamyl

*aspartase = aspartic acid

PRIMARY STRUCTURE OF PROTEINS

- Amino acid sequence of the protein chain
- Results from covalent bonding between the
amino acids in the chain (peptide bonds)
- Are translation (process from protein to DNA) of
information contained in genes.

DNA – instruction to create amino acids

3 nucleotides = Codon

SECONDARY STRUCTURE OF PROTEIN

- Peptide chains are folded regularly
- Result of hydrogen bonding between amino
acids
Hydrogen bonds = hydrogen to carbonyl

Alpha helix- stairway

Beta pleated sheet-

TERTIARY STRUCTURE OF PROTEIN

- Intact structure
- Very strong because of disulfide bonds
- Polypeptide regions

QUATERNARY STRUCTURE
- Hemoglobin
- With four indefinite globular peptide subunits:
2 identical alpha
2 identical beta