Biochemistry

1. What is Biochemistry?
- Study of the structure and properties of molecules in living organisms and how those
molecules are made, changed, and broken down.
- Biochemistry is the science in which chemistry is applied to the study of living organisms
and the atoms and molecules which comprise living organisms
2. Chiral carbon? Asymmetric carbon?
Is a carbon atom attached to 4 different atoms or groups of atoms. It is asymmetric.
3. Buffer?
A buffer is a solution that resists changes in pH when an acid or a base is added
A buffer always contains a combination of an acid – base conjugate pair
The buffer capacity is the slolution’s ability to resist pH change
4. Saturated and unsaturated fatty acid
- Saturated Fatty Acids: contain only C-C bonds, closely packed, strong attractions
between chains, high melting points, solids at room temperature.
- Unsaturated Fatty Acids: contain one or more double C=C bonds, nonlinear chains do
not allow molecules to pack closely, few interactions between chains, low melting
points, liquids at room temperature.
5. Definitions and concepts of Carbohydrates, lipids, amino acids & Proteins
* Carbohydrates are polyhydroxy aldehydes or ketones, or substances that yield such
compounds on hydrolysis.
* Lipids are non-polar compounds, soluble in organic solvents have amphipathic
properties and insoluble in water
* Amino acids are the unit produces protein that contain both amin group ( -NH2) and
carboxyl group ( -COOH)
* Proteins are a group of complex organic macromolecules and fundamental components
of all living
* Nucleic acids: molecules that store information for cellular growth and reproduction.
* Vitamins: Organic molecules need for normal metabolism in small amounts and can
not be stored in the body.
* Enzymes: a protein with catalytic properties that increases the rate of chemical
reactions without changing itself
6. Chemical linkage or bonds in Carbohydrates, lipids, amino acids & Proteins
* Carbohydrate:
+ Glucoside linkage
+ Hydrogen linkage
* Lipids:
+ Single C – C bonds.
+ Double C = C bonds.
+ Ester bonds
 * Protein
+ Peptide bonds
* Amino acid: Ionic bond
7. Chirality of an amino acid
If the amine group is located on the right side of the carbon chain, the compound is D. If
the amine group is on the left side, the molecule is L.
All of the 20 amino acids except glycine are of the L- configuration, as for all but one
amino acid the a- carbon is an asymmetric carbon. Because glycine does not contain an
asymmetric carbon atom, it is not optically active and, thus, it is neither D nor L.
8. Reaction of ninhydrin and amino acids
When 1 ml of Ninhydrin solution is added to a 1 ml protein solution and heated, the
formation of a violet color indicates the presence of α-amino acids.
9. Popular fatty acids and phospholipids
- Fatty acids: Omega – 3, Omega – 6, Trans – Fatty acids, LDL – cholesterol, HDL –
cholesterol
- Phospholipids: Lecithin
10. Oxytocin
Oxytocin is a cyclic nonapeptide, instead of having its amino acid linked in an extended
chain, two cysteine residues are joined by an S-S bond - often referred to as a disulfide
bridge. Oxytocin helps the elasticity of the uterus and stimulates contractions in females
during childbirth
11. What is pI?
The isoelectric point (pI) is the pH of the solutione at which the net charge of a protein
becomes zero
12. Structure of glycine, methionine, cysteine, tryptophan, proline, aspartic acid,
cystine, tyrosine, serine, histidine

Glycine
e

Tyrosine Tryptophane

Methionine

Histidine
Serine
Cysteine

Prolin
e Aspartic

Aspartic acid
 13. Structure of Glucose, fructose, maltose, lactose, galactose, sucrose

Fisher Harworth

Glucose

Fructose
Maltose

Lactose
Galactose

Sucrose