Proteins are unlikely to have emerged as the large, complex globular forms we know today.
First, the primordial protein synthesis machinery would inevitably have been inefficient, and …

The folding and dynamics of globular proteins is a multidimensional problem. The structures
of the heterogeneous population of refolding protein molecules are characterized by …

Molecular beacons are sensitive fluorescent probes hybridizing selectively to designated
DNA and RNA targets. They have recently become practical tools for quantitative real-time …

It is well known that the hydrophobic effect is the major factor that drives a protein toward
collapse and folding. We analyze the variation of the solvent-accessible surface area of …

Like shoelaces, the backbones of proteins may get entangled and form knots. However, only
a few knots in native proteins have been identified so far. To more quantitatively assess the …

AlloMAPS 2 is an update of the Allosteric Mutation Analysis and Polymorphism of Signalling
database, which contains data on allosteric communication obtained for predicted structures …

There were several significant milestones in the last century, from the discovery of the Bohr
effect [1] to understanding that every dynamic protein can be inherently allosteric [2, 3]. It …

Protein space is characterized by extensive recurrence, or “reuse,” of parts, suggesting that
new proteins and domains can evolve by mixing-and-matching of existing segments. From …

Rossmann folds are ancient, frequently diverged domains found in many biological reaction
pathways where they have adapted for different functions. Consequently, discernment and …

The noncoding genome plays an important role in de novo gene birth and in the emergence
of genetic novelty. Nevertheless, how noncoding sequences' properties could promote the …