Many small, monomeric proteins fold with simple two-state kinetics and show wide variation
in folding rates, from microseconds to seconds. Thus, stable intermediates are not a …

Typically, protein spatial structures are more conserved in evolution than amino acid
sequences. However, the recent explosion of sequence and structure information …

Recognition of remote homologous structures is a necessary module in AlphaFold2 and is
also essential for the exploration of protein folding pathways. Here, we propose a method …

Theoretical studies have suggested relationships between the size, stability and topology of
a protein fold and the rate and mechanisms by which it is achieved. The recent …

Proteins have dynamic structures that undergo chain motions on time scales spanning from
picoseconds to seconds. Resolving the resultant conformational heterogeneity is essential …

▪ Abstract De novo protein design has recently emerged as an attractive approach for
studying the structure and function of proteins. This approach critically tests our …

1, 3-1, 4-β-Glucanases (or lichenases, EC 3.2. 1.73) hydrolyse linear β-glucans containing β-
1, 3 and β-1, 4 linkages such as cereal β-glucans and lichenan, with a strict cleavage …

Recently, protein-folding models have advanced to the point where folding simulations of
protein-like chains of reasonable length (up to 125 amino acids) are feasible, and the major …

We use a combination of experiments, computer simulations and simple model calculations
to characterize, first, the folding transition state ensemble of the src SH3 domain, and …

The problem of how the linear amino acid sequence of a polypeptide folds to assume its
unique tertiary structure is one of the most basic and challenging conundrums of …