Protein Folding Sculpting Evolutionary Change

Protein Folding Sculpting Evolutionary Change

Our work suggests that the forces that govern protein folding exert a profound effect on how genotypes are translated into phenotypes, and that this in turn has strong effects on evolutionary processes. Molecular chaperones, also known as “heat shock proteins” (Hsps), promote the correct folding and maturation of many other proteins in the cell. Hsp90 is an abundant and highly specialized chape...

Protein folding sculpting evolutionary change.

Our work suggests that the forces that govern protein folding exert a profound effect on how genotypes are translated into phenotypes and that this in turn has strong effects on evolutionary processes. Molecular chaperones, also known as "heat-shock proteins" (Hsps), promote the correct folding and maturation of many other proteins in the cell. Hsp90 is an abundant and highly specialized chaper...

Lindquist Protein Folding Sculpting Evolutionary Change

Evolutionary Optimization of Protein Folding

Nature has shaped the make up of proteins since their appearance, [Formula: see text]3.8 billion years ago. However, the fundamental drivers of structural change responsible for the extraordinary diversity of proteins have yet to be elucidated. Here we explore if protein evolution affects folding speed. We estimated folding times for the present-day catalog of protein domains directly from thei...

Evolutionary conservation in protein folding kinetics.

The sequence and structural conservation of folding transition states have been predicted on theoretical grounds. Using homologous sequence alignments of proteins previously characterized via coupled mutagenesis/kinetics studies, we tested these predictions experimentally. Only one of the six appropriately characterized proteins exhibits a statistically significant correlation between residues'...