Structural Biochemistry/Protein/Protein Folding to New Enzymes

Protein folding to functional states resulting synthesis in the intracellular environment is a fascinating yet it is not completely understood. Substantial progress has been made in past decade in understand the fundamental nature of the mechanism of protein folding. Varies new experiments and theories were made to further understanding the “protein folding problem”, and the emerging view of folding is that it is random. The sequences of proteins folding have evolved to such complexity to be efficiently in more complex environment like inside a living cell. Proteins folding are not always “correct”. When protein folds incorrectly, this failure could lead to varies diseases.

Amyloidoses, is a group of disease resulted from incorrect protein folding. Amyloidoses include Alzheimer’s disease, which still has no treatment or cure yet; and the transmissible spongiform encephalopathies involves deposition of aggregated proteins in a variety of tissues. These diseases provide evidence that the highly organized amyloid aggregates is a generic property of polypeptides, but not a conditioned formation of proteins grouping. These grouping are uncommon to be found in normal proper functional biological systems. They are evidence to evolution, that a many different mechanisms inhibited the formation. Once the nature of the mechanisms is understood, prevention or treatments to these disease could be developed.

Citation: Biochemical Society Symposia Volume 68, Christopher M.Dobson1, Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QT, U.K.