The manner in which a newly synthesized chain of amino acids transforms itself into a
perfectly folded protein depends both on the intrinsic properties of the amino-acid sequence …

Small-angle scattering (SAS) of x-rays and neutrons is a fundamental tool in the study of
biological macromolecules. The major advantage of the method lies in its ability to provide …

This review summarises our current understanding of the underlying and universal
mechanism by which newly synthesised proteins achieve their biologically functional states …

As was noted in our recent review, 1 the protein folding field underwent a cyclic
development. Initially, protein folding was viewed as a strictly experimental field belonging to …

During the process of protein folding, the amino acid residues along the polypeptide chain
interact with each other in a cooperative manner to form the stable native structure. The …

The ability of protein chains to spontaneously form their three-dimensional structures is a
long-standing mystery in molecular biology. The most conceptual aspect of this mystery is …

Coarse-grained, self-contained polymer models are powerful tools in the study of protein
folding. They are also essential to assess predictions from less rigorous theoretical …

Newly synthesised proteins need to fold, often to intricate and close-packed structures, in
order to function. The underlying mechanism by which this complex process takes place …

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 …

We studied the microsecond folding dynamics of three β hairpins (Trp zippers 1–3, TZ1–
TZ3) by using temperature-jump fluorescence and atomistic molecular dynamics in implicit …