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

Although protein-folding studies began several decades ago, it is only recently that the tools
to analyze protein folding at the single-molecule level have been developed. Advances in …

Using a genetic selection we identified mutants of the M. janaschii tyrosyl-tRNA synthetase
that selectively charge an amber suppressor tRNA with para-propargyloxyphenylalanine in …

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 …

Protein surface hydration is fundamental to its structural stability and flexibility, and water−
protein fluctuations are essential to biological function. Here, we report a systematic global …

Microreactor technology has gained significant popularity in the chemical and process
industry in the past decade. The development of microreactors either as innovative …

Unfolded proteins under strongly denaturing conditions are highly expanded. However,
when the conditions are more close to native, an unfolded protein may collapse to a …

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 …

Globular proteins often exhibit cooperative unfolding transitions in which only folded (native)
and unfolded (denatured) molecules are populated at equilibrium. 1, 2 This two-state …

The increasingly narrow and brilliant beams at X-ray facilities reduce the requirements for
both sample volume and data acquisition time. This creates new possibilities for the types …