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Introduction to biochemistry
Moshtaghi-Kashanian
Associated professor
Kerman University of Medical Sciences
What is Biochemistry
Biochemistry is mother of different field in medicine
1.
2.
3.
4.
5.
6.
7.
8.

Anatomy
Physiology
Pharmacology
Genetic
Immunology
Bacteriology
Immunology
Parasitology

1.
2.
3.
4.
5.
6.
7.

Internal medicine
Surgery
Endocrinology
Dentistry
Psychology
Sociology
Nursing
Definition of Biochemistry
“Chemistry of Life”
Living Things are composed of lifeless molecules
Doesn’t fully take into account what chemistry is
Biochemistry- Study of the structure, properties and
changes of bio-matter
Special Considerations
1. Complex and highly ordered
2. Everything has a function
3. Living things transform their environment
(extract energy)
4. Self-replicating
5. Reactions occur at constant temperature,
pressure and pH; in an aqueous environment
Biomolecules - Elements
C, H, O, N

99% of mass of most cells

P, S
Mg2+, Na+, K+, Ca2+, ClFe, Zn, Mn, Co, Cu
Biomolecules - Macromolecules
1. Carbohydrates- made up mostly of 7
monosaccharides
2. Proteins - 5 × 106, made up of 20 amino acids
3. Nucleic Acids - 1,000, made up of 4 nucleotides
4. Lipids
Water
•
•

70% of most organisms
polar
•
•

favors solubility
directionality holds macromolecules in given
conformations
Water
•

hydrogen bond
•
•

•
•
•

half-life < 1/1,000,000 sec
holds water together without being viscous

high specific heat
colligative properties
weakly ionizable
Sizes of living things
Cell Structure
Cell Membrane
Appears as 3 layers by EM
• 7.5-10 nm thick
• “Unit membrane”
These three things are explained on
a molecular level as a
phospholipid bilayer
Function: osmotic barrier
Present in all cells
Further consideration in lipid
material.
•
Nucleus
Bounded by a porous
nuclear membrane
Function: contain DNA
Present in all eukaryotic
cells
• 1 per cell
• Often 1-4 nucleoli
•
The nucleus and the nuclear envelope
Cell Wall & cell membrane
Thick, tough wall
Function: rigidity
Present in plant and prokaryotic cells
Animal cell anatomy
Plant cell anatomy
Mitochondria
•
•

Shape varies, size varies
500-2,000 per cell
Mitochondria
Function: “powerhouse of the cell”
Present in all eukaryotic cells
Structure: compartments
Further consideration in metabolism.
Endoplasmic Reticulum
Rough and Smooth
Phospholipid bilayer surrounding a lumen ± ribosomes
Function: protein synthesis (rough) lipid synthesis (smooth)
Present in all eukaryotic cells (lots)
Rough Endoplasmic Reticulum
Surface looks rough because of the presence of ribosomes,
another organelle (present in all cells)
Golgi Apparatus
Historically cis, medial and
trans: trans-golgi network
Function: protein processing
and secretion
Present in all eukaryotic cells
(lots)
Lysosomes
About as big as a
mitochondrion
• not much to see
Function: degradation of
proteins
Present in animal cells, plant
cells have similar organelle
called peroxisome
Number per cell varies
enormously
•
Chloroplasts
Stacks of “grana”
• grana composed of
thylakoid disks
Function: photosynthesis
Present in photosynthetic
cells
50-200 per cell
•
Cytoplasm
Aqueous, solute-containing contents within the plasma
membrane
Contains soluble proteins, salts, organelles
Cytosol- is the supernate of a centrifugation process
Microtubules
•
•

Polymer of a protein called actin
Gives shape to cell, also functions in transport
around the cell
4 classes of macromolecules
Carbohydrates: Energy,
structure
Lipids: Energy, membranes
Proteins: Catalysts, structure,
etc.
Nucleic Acids: Information
Macromolecules: Carbohydrates

Glucose isomers
Macromolecules: Carbohydrates

Carbohydrates
Polymerization

glucose

fructose

sucrose
Making & breaking polymers
Storage polysaccharides
starch

glycogen
Cellulose: A structural polysaccharide
Chitin: a structural polysaccharide
Fatty acids &
triacylglycerol
Cholesterol:
a steroid
Polar & charged amino acids
Nonpolar amino acids
Macromolecules: Proteins
Structural proteins
Protein Structure: 4 Levels
Primary
Secondary
Tertiary
Quaternary
Primary structure of protein:
the amino acid sequence

lysozyme
Amino Acid Structure

R is different for different amino acids.
Polymerization
is peptide bond
formation
Primary structure of protein:
the amino acid sequence

Primary structure is due to strong
covalent peptide bonds joining amino
acids together.
lysozyme
Secondary structure:
group of amino acids
folded repetitively to
make a discrete shape.

lysozyme
Secondary structure:
group of amino acids
folded repetitively to
make a discrete shape.

due to hydrogen
bonds between
amino acids’
backbones.
lysozyme
Tertiary
structure:
the overall 3-d
conformation of
a polypeptide.

lysozyme
Tertiary
structure
involves several
kinds of bonds.
Tertiary Structure
Most proteins are
hydrophilic outside,
hydrophobic inside.
Macromolecules: Nucleic Acids

Deoxyribonucleic
Acid
Nucleic Acids are Polymers
pH and Buffers
Water is Weakly Ionizable
•
•
•
•

2 H2O <===> OH– + H3O+
Weakly means this doesn’t happen often
[OH–] = [H3O+] = 1 × 10-7 M,
[OH–] × [H3O+] = 1 × 10-14, the basis of the pH
scale
Equilibrium Constants
Mathematically Represent Degree of
Dissociation in biochemistry to
Keq’ is used
denote modified standard
state.
pKa’ Values are Used to Describe
Ionization of Acids
•
•
•
•

CH3COOH + H2O <===> CH3COO– + H3O+
Keq’ =
Ka’ = 1.74 x 10-5 =
pKa’ = 4.76
Graphical Determination of pKa’
•

The pKa’ is the pH at the
point where buffering
occurs
Buffers
Buffer- a compound that does not allow the pH to
change even if acid or base is added to the system.
Amphiprotic compounds are also good buffers.
Amphiprotic compound- a compound that can act as
a proton donor or as a proton acceptor.
The Henderson-Hasselbalch Equation
is Used to Determine the pH of
Buffered Solutions
pH = pKa’ + log

[A–]
[HA]

or pH = pKa’ + log

[salt]
[acid]
When pH = pKa’, There is Equal
Amounts of A– and HA

•

Proof on board
pH Problems
What will the pH of a solution be if 0.1 mL of 6 M
HCl is added to 100. mL of H2O?
What will the pH of a solution be if 0.1 mL of 6 M
HCl is added to 100. mL of 1 M HEPES initially
at pH 7.6?
What will the pH of a solution be if 0.1 mL of 6 M
HCl is added to 100. mL of 50 mM HEPES
initially at pH 7.6?
Choosing a Buffer
•
•
•

pKa ± 0.5 pH units
ionic strength: use 50 or 100 mM
metal ion chelation, etc.

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