Introduction to biochemistry

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
 What is Biochemistry
Biochemistry is mother of different field in medicine

1. Anatomy 1. Internal medicine

2. Physiology 2. Surgery
3. Pharmacology 3. Endocrinology
4. Genetic 4. Dentistry
5. Immunology 5. Psychology
6. Bacteriology 6. Sociology
7. Immunology 7. Nursing
8. Parasitology
 Biomolecules - Elements
C, H, O, N 99% of mass of most cells

P, S
Mg2+, Na+, K+, Ca2+, Cl-
Fe, 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:

lysozyme
 Amino Acid Structure

R is different for different amino acids.

Polymerization
peptide
bond
formation
 Primary structure of protein:

Primary structure is due to strong

covalent peptide bonds joining amino
acids together.
lysozym
Secondary structure:
of amino acids
repetitively to discrete
shape.

lysozyme
Secondary structure:
of amino acids
repetitively to 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