Fig. 5-22c
Normal red blood
cells are full of
individual
hemoglobin
molecules, each
carrying oxygen.
Fibers of abnormal
hemoglobin deform
red blood cell into
sickle shape.
10 µm
10 µm
Slide 92
What Determines Protein Structure?
In addition to primary structure, physical and chemical conditions can affect structure
Alterations in pH, salt concentration, temperature, or other environmental factors can cause a protein to unravel
This loss of a protein’s native structure is called denaturation
A denatured protein is biologically inactive
Slide 93
Fig. 5-23
Normal protein
Denatured protein
Denaturation
Renaturation
Slide 94
Protein Folding in the Cell
It is hard to predict a protein’s structure from its primary structure
Most proteins probably go through several states on their way to a stable structure
Chaperonins are protein molecules that assist the proper folding of other proteins
Slide 95
Fig. 5-24
Hollow
cylinder
Cap
Chaperonin
(fully assembled)
Polypeptide
Steps of Chaperonin
Action:
An unfolded poly-
peptide enters the
cylinder from one end.
1
2
3
The cap attaches, causing the
cylinder to change shape in
such a way that it creates a
hydrophilic environment for
the folding of the polypeptide.
The cap comes
off, and the properly
folded protein is
released.
Correctly
folded
protein
Slide 96
Fig. 5-24a
Hollow
cylinder
Chaperonin
(fully assembled)
Cap
Slide 97
Fig. 5-24b
Correctly
folded
protein
Polypeptide
Steps of Chaperonin
Action:
1
2
An unfolded poly-
peptide enters the
cylinder from one end.
The cap attaches, causing the
cylinder to change shape in
such a way that it creates a
hydrophilic environment for
the folding of the polypeptide.
The cap comes
off, and the properly
folded protein is
released.
3
Slide 98
Scientists use X-ray crystallography to determine a protein’s structure
Another method is nuclear magnetic resonance (NMR) spectroscopy, which does not require protein crystallization
Bioinformatics uses computer programs to predict protein structure from amino acid sequences