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Protein and RNA folding develops on many different timescales ranging from nanoseconds to seconds.  While the longest times have been probed experimentally for many years, only in the past decade have advances in laser spectroscopy allowed a view into dynamics faster than 1 millisecond.

 

 

 

Within the cell, proteins are continuously constructed from amino acid building blocks strung together like beads on a necklace using a gene as a template for the sequence.

 

 

 

 

 

But a protein does nothing until this necklace folds into the native structure necessary for performing its particular function.

The process of folding a protein into its native structure is spontaneous and depends in detail on the physical interactions between different residues of the polypeptide chain and with the surrounding water. 

Text Box: The interior of a cell is a very diverse and crowded environment and a folding protein is always in danger of misfolding and aggregating.  Alzheimer’s disease and type-II diabetes are part of a growing class of diseases due to protein aggregation.  Given the apparent toxicity of disordered aggregants of even common proteins, there is enormous evolutionary pressure for proteins that fold quickly and efficiently.  

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

RNA’s are another set of macromolecules essential for life, having perhaps an even wider range of roles in the cell than proteins.  RNA is best known as the template in protein synthesis, but some ribozymes also have catalytic activity; most of the functional part of the ribosome is comprised of RNA.