Microfabricated integrated circuits revolutionized computation by vastly reducing the space,
labor, and time required for calculations. Microfluidic systems hold similar promise for the …

Proteins exhibit structural fluctuations over decades of time scales. From the picosecond
side chain motions to aggregates that form over the course of minutes, characterizing protein …

The breadth of structure and function displayed by the molecules of biology is remarkable.
Considering that there are only three major biopolymer backbones (proteins, ribonucleic …

The structure of a protein complex together with information about its affinity and other
thermodynamic characteristics provide a “frozen” view of the complex. This picture ignores …

How fast can a protein possibly fold? This question has stimulated experimentalists to seek
fast folding proteins and to engineer them to fold even faster. Proteins folding at or near the …

Cells face a constant challenge as they produce new proteins. The newly synthesized
polypeptides must be folded properly to avoid aggregation. If proteins do misfold, they must …

15N relaxation dispersion experiments were applied to the isolated N-terminal SH3 domain
of the Drosophila protein drk (drkN SH3) to study microsecond to second time scale …

Terahertz (THz) spectroscopic investigations of condensed‐phase biological samples are
reviewed ranging from the simple crystalline forms of amino acids, carbohydrates and …

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 …

Formation of a specific contact between two residues of a polypeptide chain is an important
elementary process in protein folding. Here we describe a method for studying contact …