The University of North Carolina at Chapel Hill, Chapel Hill, NC, USA. This talk will provide
an overview of new approaches to study and manipulate signaling in living cells and …

An outstanding challenge in the field of molecular biology has been to understand the
process by which proteins fold into their characteristic three-dimensional structures. Here …

The argument that the hydrophobic effect is the primary effect driving the folding of globular
proteins is nearly universally accepted (including by the authors). But does this view also …

We compared folding properties of designed protein Top7 and natural protein S6 by using
coarse-grained chain models with a mainly native-centric construct that accounted also for …

A complete understanding of protein function and dynamics requires the characterization of
the multiple thermodynamic states, including the denatured state ensemble (DSE). Whereas …

Live imaging of genome has offered important insights into the dynamics of the genome
organization and gene expression. The demand to image simultaneously multiple genomic …

As proposed here, β‐turns play an essential role in protein self‐assembly. This compact,
four‐residue motif affects protein conformation dramatically by reversing the overall chain …

Three-dimensional structures of proteins are the support of their biological functions. Their
folds are stabilized by contacts between residues. Inner protein contacts are generally …

Understanding protein folding mechanisms and their sequence dependence requires the
determination of residue-specific apparent kinetic rate constants for the folding and …

Small proteins with globular structures often fold by simple all-or-none mechanisms, both in
an equilibrium and a kinetic sense, despite the very large number of partly folded …