BIOLOGICAL

MOLECULES
WAHYUNI PUJI
ASTUTI

SMAN 3 MADIUN
 LEARNING OBJECTIVES

Describe the structure of amino acids and the way in

which peptide bonds are made and broken
Describe the primary structure of polypeptides and
protein and how it affects their secondary and
tertiary structure
Explain that the quaternary structure of protein is
formed
Describe the importance of hydrogen bonds,
disulphide bonds, ionic bonds and hydrophobic
interactions in maintaining three dimensional
structure of protein
 LEARNING OBJECTIVES

Discuss the ways in which the structures of

haemoglobin and collagen are related to their
functions
STRUCURE OF AMINO ACIDS
 PROPERTIES
Amino acids have different sizes and shapes
They posses properties such as:
• Acidic
• Basic
• Polar
• Aromatic
• Hydrophobic
VARIOUS OF AMINO ACIDS
VARIOUS OF AMINO ACIDS
PEPTIDE BOND FORMATION
PEPTIDE BOND
PRIMERY & SECONDARY STRUCTURE
 Primary Assembly
STRUCTURE

PROCESS
Secondary Folding

Packing
Tertiary

Interaction
Quaternary
 PRIMARY
STRUCTURE

• linear
• ordered
• 1 dimensional
• sequence of amino acid polymer
 SECONDARY
STRUCTURE

• non-linear
• 3 dimensional
• Localized to regions of an amino acid
chain
• formed and stabilized by hydrogen
bonding, electrostatic and van der Waals
interactions
 TERTIARY
STRUCTURE

• Non-linear
• 3 dimensional
• Global but restricted to the amino acid polymer
• Formed and stabilized by hydrogen bonding,
covalent (e.g. disulfide) bonding, hydrophobic
packing toward core and hydrophilic exposure
to solvent
• A globular amino acid polymer folded and
compacted is somewhat functional (catalytic)
• Non-linear
• 3 dimensional
• Global, and across distinct amino acid
polymers
• Formed by hydrogen bonding, covalent
bonding, hydrophobic packing and
hydrophilic exposure
• Involves interaction among tertiary
structure elements of separate polymer
chains
• Globular proteins, e.g. hemoglobin,
largely involved in catalytic roles
• Fibrous proteins, e.g. collagen,
largely involved in structural roles