Protein Folding, Aggregation and DesignConcepts, Experiments, Theories and Mechanisms

Proteins are one of the key building blocks of biology and perhaps the most versatile and complex class of biological molecule in terms of structure and function. Synthesized as linear chains of amino acids from the ribosome, they come in (at least) millions of different combinations of just 20 amino... read moreacids. It is remarkable how these linear chains can fold into functional units that catalyse most cellular reactions, form the structural scaffolds, operate cellular transportation, signalling, synthesis and almost everything else required to run living systems.

One of the great challenges in understanding proteins has been in fact how they fold. Proteins are highly prone to misfolding relative to other classes of biomolecules and as such can inappropriately aggregate which is associated with a wide range of neurodegenerative diseases. While many simple proteins can fold reversibly on their own, more than two thirds of the proteome cannot and must be guided by an elaborate quality control system.

The scope of this series covers the spectrum of fundamental protein behaviour from the theory of how they fold to how they are managed upon synthesis in the cell to how they misfold and aggregate in disease and cause damage to cellular function. We also cover some of the new exciting areas in protein engineering to take advantage of their great diversity and malleability for practical use.

This series was originally created in 2007, with Dr. Caroline Wright as Editor. An update of the series was undertaken in 2016 with a new Editor, Prof. Danny Hatters.