Sandbox Reserved 197: Difference between revisions
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==='''Summary'''=== | ==='''Summary'''=== | ||
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, | 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, mutating proteins greatly effects the stability of the molecule and the rate of folding. | ||
=='''Medical Importance'''== | =='''Medical Importance'''== | ||
