As a protein is being synthesized, the correct folding of the protein is aided b
ID: 85765 • Letter: A
Question
As a protein is being synthesized, the correct folding of the protein is aided by the movement of some amino acids toward the inner areas of the protein and others toward exterior of the protein. Why? What does this do structurally and functionally for the molecule? Give 2 specific examples of the folding within different types of proteins. (5 pts) As a protein is being synthesized, the correct folding of the protein is aided by the movement of some amino acids toward the inner areas of the protein and others toward exterior of the protein. Why? What does this do structurally and functionally for the molecule? Give 2 specific examples of the folding within different types of proteins. (5 pts)Explanation / Answer
As a protein is being synthesized, the correct folding of the protein is aided by the movement of some amino acids
toward the inner areas of the protein and others toward exterior of the protein.
Because it has both Hypdrophillic and hydrophobic groups of amino acids.
Folding of the protein is aided by the movement of some amino acids toward the inner areas of the protein is due
to hydrophobic group. The exclusion of hydrophobic groups from the aqueous surface is called the Hydrophobic
Effect.
Folding of the protein is aided by the movement of amino acids toward exterior of the protein is due to Hydrophilic
group which remains on aqueous surface.
Protein folding provides its functional shape or conformation.
Specific examples of the folding-
1) 4-helix bundle Folding - Four-helix bundles typically consist of four helices packed in a coiled-coil arrangement.
ln this proteins the interfaces between the helices consist mostly of hydrophobic residues while polar side chains
on the exposed surfaces interact with the aqueous environment.
2) Reversible folding - The reversible folding of a protein depends on free energy. eg: For the alpha helix proteins
two-state process is followed. The two-state reaction involves a partly unfolded state and a folded bR
(bacteriorhodopsin) state.
3) Rossman folding - This is a coenzyme-binding folds of some dehydrogenases.
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