Sandbox Reserved 197: Difference between revisions

Protein folding is not due to one interaction, but a network of interactions within the protien. Presence of Cu+ upon folding shows that the Cu+ does not dictate folding, but rather binds to a pre-existing structure, therefore protein folding is not due to external forces. When a proline or disulfide bond is removed, the structural changes are usually confined to the site of mutation and minor structural changes occur within close proximity to the mutation. Mutation of a ''cis'' proline is often accompanied by an insertion or deletion in order to provide more flexibility for the structure. Although the effects of mutations seem to be localized, replacing proteins greatly effects the stability of the molecule and the rate of folding.

Protein folding has several medical implications. Diseases such as ALS, Alzheimer's Disease, and Parkinson's Disease can all be traced back to protein folding because proteins can form aberrant aggregates when they do not fold correctly.  This abnormaility can be toxic to human nerve cells.  During folding, proteins sometimes make mistakes.  Each protein contains <scene name='Sandbox_Reserved_197/Hydrophobic-hydrophilic/1'>hydrophobic and hydrophilic residues</scene>.  The hydrophilic residues lie on the outer part of the protein and the hydrophobic residues bury themselves due to the hydrophobic effect [http://en.wikipedia.org/wiki/Hydrophobic_effect]. In the case of these aggregates, the mistake exposes "sticky" <scene name='Sandbox_Reserved_197/Hydrophobic/1'>hydrophobic patches</scene> of the interior that can cause several proteins to stick to one another.  In the future researchers hope to design drugs that combat mistakes in protein folding.  The use of ribonuclease A in protein folding research has been an instrumental feature in designing experiments to determine these "misfolding" snapshots and in developing therapies to prevent this problem in the future.