Natural evolution has yielded enzymes that catalyze virtually all metabolic reactions under
mild conditions with high specificities and enormous rate enhancements. 1 It has been a …

Theoretical and experimental studies of protein folding have suggested that the topology of
the native state may be the most important factor determining the folding pathway of a …

The amino acid sequences of proteins have evolved over billions of years, preserving their
structures and functions while responding to evolutionary forces. Are there conserved …

Protein sequence, structure, and function are inherently linked through evolution and
population genetics. Our knowledge of protein structure comes from solved structures in the …

The studies of the folding of structurally related proteins have proved to be a very important
tool for investigating protein folding. Here we review some of the insights that have been …

Triosephosphate isomerase (TIM) barrel proteins have not only a conserved architecture
that supports a myriad of enzymatic functions, but also a conserved folding mechanism that …

The βα-repeat class of proteins, represented by the (βα) 8 barrel and the α/β/α sandwich, are
among the most common structural platforms in biology. Previous studies on the folding …

To test the roles of motif and amino acid sequence in the folding mechanisms of TIM barrel
proteins, hydrogen-deuterium exchange was used to explore the structure of the stable …

The structures of partially folded states appearing during the folding of a (βα) 8 TIM barrel
protein, the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus (sIGPS), was …

Temperature is one of the main variables that modulate protein function and stability.
Thermodynamic studies of oligomeric proteins, the dominant protein natural form, have been …