The study of proteins with the same architecture, but different sequence has proven to be a valuable tool in the protein folding field. As a prelude to studies on the folding mechanism of spectrin domains we present the kinetic characterisation of the wild-type forms of the 15th, 16th, and 17th domains of chicken brain alpha-spectrin (referred to as R15, R16 and R17, respectively). We show that...

Although protein folding and stability have been well explored under simplified conditions in vitro, it is yet unclear how these basic self-organization events are modulated by the crowded interior of live cells. To find out, we use here in-cell NMR to follow at atomic resolution the thermal unfolding of a β-barrel protein inside mammalian and bacterial cells. Challenging the view from in vitro...

ATP-dependent proteases control the concentrations of hundreds of regulatory proteins and remove damaged or misfolded proteins from cells. They select their substrates primarily by recognizing sequence motifs or covalent modifications. Once a substrate is bound to the protease, it has to be unfolded and translocated into the proteolytic chamber to be degraded. Some proteases appear to be promis...

Joint remembering relies on the successful interweaving of multiple cognitive, linguistic, bodily, social and material resources, anchored in specific cultural ecosystems. Such systems for joint remembering in social interactions are composed of processes unfolding over multiple but complementary timescales which we distinguish for analytic purposes with the terms ‘coordination’, ‘collaboration...

Human telomeric DNA consists of tandem repeats of the sequence 5'-TTAGGG-3' that can fold into various G-quadruplexes, including the hybrid, basket, and propeller folds. In this report, we demonstrate use of the α-hemolysin ion channel to analyze these subtle topological changes at a nanometer scale by providing structure-dependent electrical signatures through DNA-protein interactions. Whereas...

Statistical analyses of forced unfolding data for protein tandems, i.e., unfolding forces (force-ramp) and unfolding times (force-clamp), used in single-molecule dynamic force spectroscopy rely on the assumption that the unfolding transitions of individual protein domains are independent (uncorrelated) and characterized, respectively, by identically distributed unfolding forces and unfolding ti...

We show that the hypercube has a face-unfolding that tiles space, and that unfolding has an edge-unfolding that tiles the plane. So the hypercube is a “dimension-descending tiler.” We also show that the hypercube cross unfolding made famous by Dali tiles space, but we leave open the question of whether or not it has an edge-unfolding that tiles the plane.

The deflection of a cantilever is measured using a laser beam and position-sensing detector to obtain force and displacement for both imaging and force spectroscopy. In force spectroscopy, the cantilever is attached to one end of the protein or DNA sample while the other end is immobilized on the surface. The force and position of the tip are measured as the surface is moved away from the tip, ...

An effective free energy potential, developed originally for binding free energy calculation, is compared to calorimetric data on protein unfolding, described by a linear combination of changes in polar and nonpolar surface areas. The potential consists of a molecular mechanics energy term calculated for a reference medium (vapor or nonpolar liquid), and empirical terms representing solvation a...