Proteins

The 411
• 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
• Most important, protein enzymes function as
catalysts in cells, regulating metabolism by
selectively accelerating chemical reactions without
being consumed.
 Amino Acids
• Small – molecules (20 variants)
– 1 Amino group
– 1 Carboxyl Group
– 1 “R” Group
– Amino acids differ in their properties due to
differing side chains, called R groups
• Joined by Peptide Bonds to form Polypeptides
– A protein consists of one or more polypeptides
– Each polypeptide has a unique linear sequence of
amino acids
Fig. 5-UN1

Alpha carbon

Amino Carboxyl
group group
 How to Make Proteins!
DNA T A C C G C T C C G C C G T C G A C A A T A C C A C T

mRNA ____________________________________________________________________________

tRNA____________________________________________________________________________

AA ____________________________________________________________________________
Fig. 5-17a

Nonpolar

Glycine Alanine Valine Leucine Isoleucine

(Gly or G) (Ala or A) (Val or V) (Leu or L) (Ile or I)

Methionine Phenylalanine Tryptophan Proline

(Met or M) (Phe or F) (Trp or W) (Pro or P)

What makes all Amino Acids different?

Fig. 5-17b

Polar

Serine Threonine Cysteine Tyrosine Asparagine Glutamine

(Ser or S) (Thr or T) (Cys or C) (Tyr or Y) (Asn or N) (Gln or Q)
Fig. 5-17c

Electrically
charged
Acidic Basic

Aspartic acid Glutamic acid Lysine Arginine Histidine

(Asp or D) (Glu or E) (Lys or K) (Arg or R) (His or H)
Fig. 5-18

Peptide
Polypeptide Formation
bond

(a)

Side chains
Peptide
bond

Backbone

Amino end Carboxyl end

(b) (N-terminus) (C-terminus)
 Structure

Groove
Groove
 Levels of Structure
• The primary structure
– Unique sequence of amino acids
• Secondary structure
– Found in most proteins, consists of coils and folds in the
polypeptide chain due to Hydrogen Bonding
• Tertiary structure
– Determined by interactions among various side chains (R
groups)
– Fully Folded
• Quaternary structure
– Results when a protein consists of multiple polypeptide chains
 Primary Structure Primary
1

H3N
+
5
• Primary structure, the
Amino end sequence of amino
acids in a protein, is
10 like the order of letters
in a long word
15 Amino acid
subunits • Primary structure is
20
determined by
inherited genetic
information
25
Fig. 5-21c

Secondary Structure
Beta pleated sheet

Examples of
amino acid
subunits

• The coils and folds of secondary

structure result from hydrogen
alpha helix bonds between repeating
constituents of the polypeptide
backbone
• Typical secondary structures are
a coil called an  helix and a
folded structure called a 
pleated sheet
Fig. 5-21f
Hydrophobic
interactions and
van der Waals
interactions

Polypeptide
backbone
Hydrogen
bond

Disulfide bridge

Ionic bond

Tertiary
 Quaternary
• 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
Fig. 5-21g

Polypeptide  Chains
chain

Iron
Heme

 Chains
Hemoglobin
Collagen
Fig. 5-22
Normal hemoglobin Sickle-cell hemoglobin
Val His Leu Thr Pro Glu Glu
Primary
Primary Val His Leu Thr Pro Val Glu
structure
structure 1 2 3 4 5 6 7 1 2 3 4 5 6 7

Exposed
Secondary Secondary hydrophobic
and tertiary  subunit and tertiary region  subunit
structures structures

 


Quaternary Normal Quaternary Sickle-cell
structure hemoglobin structure hemoglobin
(top view) 

 

Function Molecules do Function Molecules

not associate interact with
with one one another and
another; each crystallize into
carries oxygen. a fiber; capacity
to carry oxygen
is greatly reduced.

10 µm 10 µm

Red blood Normal red blood Red blood Fibers of abnormal

cell shape cells are full of cell shape hemoglobin deform
individual red blood cell into
hemoglobin sickle shape.
moledules, each
carrying oxygen.