The Structure and Function

of Biomolecules
(continued)
Proteins
 Proteins have many structures,
resulting in a wide range of functions
• Proteins account for more than 50% of the dry mass of
most cells
• Protein functions include structural support, storage,
transport, cellular communications, movement, and
defense against foreign substances
• Enzymes are a type of protein that acts as a catalyst,
speeding up chemical reactions
• Enzymes can perform their functions repeatedly,
functioning as workhorses that carry out the processes
of life
 Polypeptides
• A protein consists of one or more polypeptides
• Polypeptides are polymers of amino acids
 Amino Acid Monomers
• Amino acids are organic molecules with carboxyl and
amino groups
• Amino acids differ in their properties due to differing
side chains, called R groups
• Cells use 20 amino acids to make thousands of proteins
 a carbon

Amino Carboxyl
group group
 Glycine (Gly) Alanine (Ala) Valine (Val) Leucine (Leu) Isoleucine (Ile)

Nonpolar

Methionine (Met) Phenylalanine (Phe) Tryptophan (Trp) Proline (Pro)

Polar

Serine (Ser) Threonine (Thr) Cysteine (Cys) Tyrosine (Tyr) Asparagine (Asn) Glutamine (Gln)
 Acidic Basic

Electrically
charged

Aspartic acid (Asp) Glutamic acid (Glu) Lysine (Lys) Arginine (Arg) Histidine (His)
 Amino Acid Polymers
• Amino acids are linked by peptide bonds
• A polypeptide is a polymer of amino acids
• Polypeptides range in length from a few monomers to
more than a thousand
• Each polypeptide has a unique linear sequence of
amino acids
• The amino acid sequences of polypeptides were first
determined by chemical methods
• Most of the steps involved in sequencing a polypeptide
are now automated
 Protein Conformation and Function
• A functional protein consists of one or more
polypeptides twisted, folded, and coiled into a unique
shape
• The sequence of amino acids determines a protein’s
three-dimensional conformation
• A protein’s conformation determines its function
• Ribbon models and space-filling models can depict a
protein’s conformation
 Groove

A ribbon model

Groove

A space-filling model
 Four Levels of Protein Structure
• The primary structure of a protein is its unique
sequence of amino acids
• Secondary structure, found in most proteins, consists
of coils and folds in the polypeptide chain
• Tertiary structure is determined by interactions among
various side chains (R groups)
• Quaternary structure results when a protein consists of
multiple polypeptide chains
 b pleated sheet
+H
3N
Amino end Amino acid
subunits

a helix
1. Primary Structure Amino end Amino acid
subunits

• Primary structure, the

sequence of amino
acids in a protein, is
like the order of
letters in a long word
• Primary structure is
determined by
inherited genetic
information

Carboxyl end
 2. Secondary Structure
• The coils and folds of secondary structure result from hydrogen
bonds between repeating constituents of the polypeptide
backbone
• Typical secondary structures are a coil called an alpha helix and a
folded structure called a beta pleated sheet
b pleated sheet

Amino acid
subunits

a helix
 3. Tertiary Structure

• Tertiary structure is
determined by
interactions between R
groups, rather than
interactions between
backbone constituents
Hydrophobic
• These interactions interactions and
van der Waals
between R groups include interactions
hydrogen bonds, ionic Polypeptide

bonds, hydrophobic Hydrogen

backbone

interactions, and van der bond

Waals interactions
• Strong covalent bonds Disulfide bridge

called disulfide bridges

may reinforce the Ionic bond
protein’s conformation
 4. Quaternary Structure
• Quaternary structure results when two or more polypeptide chains
form one macromolecule
• Collagen is a fibrous protein consisting of three polypeptides coiled
like a rope
• Hemoglobin is a globular protein consisting of four polypeptides: two
alpha and two beta chains Polypeptide
chain b Chains

Iron
Heme

a Chains
Polypeptide chain Collagen Hemoglobin
 What Determines Protein
Conformation?
• In addition to primary structure, physical and chemical
conditions can affect conformation
• Alternations in pH, salt concentration, temperature, or
other environmental factors can cause a protein to
unravel
• This loss of a protein’s native conformation is called
denaturation
• A denatured protein is biologically inactive
 Denaturation

Normal protein Denatured protein

Renaturation