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 …

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 relative contributions of chain topology and amino acid sequence in directing the folding
of a (βα) 8 TIM barrel protein of unknown function encoded by the Bacillus subtilis iolI gene …

The triosephosphate isomerase (TIM) barrel protein fold is a structurally repetitive
architecture that is present in approximately 10% of all enzymes. It is generally assumed that …

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 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 …

Non-local hydrogen bonding interactions between main chain amide hydrogen atoms and
polar side chain acceptors that bracket consecutive βα or αβ elements of secondary …

The conservation of the intrinsic dynamics of proteins emerges as we attempt to understand
the relationship between sequence, structure and functional conservation. We characterise …

Despite efforts for over 25 years, de novo protein design has not succeeded in achieving the
TIM-barrel fold. Here we describe the computational design of four-fold symmetrical (β/α) 8 …

Abstract The (βα) 8/TIM barrel is one of the most common folds of known protein structures
facilitating diverse catalytic functions. The fold is formed by the repetition of the basic βαβ …