Tertiary Structure of Proteins
(Cooper, 1997 p. )
Tertiary structure is the further folding of a protein molecule where
diverse parts of the molecule are held together and interact between r-groups
via the following types of bonds:
-
Hydrogen bond
-
Hydrophobic interactions
-
Ionic bonds
-
Disulfide bonds
Tertiary folding of polypeptides determines the three-dimensional structure
of the protein.
Explore the tertiary of the three dimensional structure of small protein,
ribonuclease.
(Note: to view ribonuclease interactively on your Web browser, the free
Chemscape Chime plug-in viewer must be installed in your browser's plug-in
folder.) Be sure to select the options and view the hydrogen and disulfide
bonds. This will show how the helicies and sheets are held together
in three dimensional space.
References:
Cooper, Geoffrey M. (1997) The Cell: A Molecular Approach; ASM Press,
Washington, D.C. / Sinauer Associates, Inc., Sunderland, MA.