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Single-protein force experiments have relied on a molecular fingerprint based on tethering multiple single-protein domains in a polyprotein chain. However, correlations between these domains remain an issue in interpreting force spectroscopy data, particularly during protein folding. Here we first show that force-clamp spectroscopy is a sensitive technique that provides a molecular fingerprint based on the unfolding step size of four single-monomer proteins. We then measure the force-dependent unfolding rate kinetics of ubiquitin and I27 monomers and find a good agreement with the data obtained for the respective polyproteins over a wide range of forces, in support of the Markovian hypothesis. Moreover, with a large statistical ensemble at a single force, we show that ubiquitin monomers also exhibit a broad distribution of unfolding times as a signature of disorder in the folded protein landscape. Furthermore, we readily capture the folding trajectories of monomers that exhibit the same stages in folding observed for polyproteins, thus eliminating the possibility of entropic masking by other unfolded modules in the chain or domain-domain interactions. On average, the time to reach the I27 folded length increases with increasing quenching force at a rate similar to that of the polyproteins. Force-clamp spectroscopy at the single-monomer level reproduces the kinetics of unfolding and refolding measured using polyproteins, which proves that there is no mechanical effect of tethering proteins to one another in the case of ubiquitin and I27.

Jammed matter is by definition impenetrable to light, such that little is known about the geometry of jammed systems. Using confocal microscopy to image an emulsion in 3D, we first explain the origin of the enhanced fluorescence at the droplet contacts and then determine the contact network inside the model frictionless system. This enables the experimental determination of the average coordination number which agrees with the isostatic predicted value of approximately 6. Furthermore, we calculate the entropy of the packing from the network of contacts.

A system's equilibrium variance can be analyzed to probe its underlying dynamics at higher resolution. Here, using single-molecule atomic-force microscope techniques, we show how the variance in the length of a single dextran molecule can be used to establish thermodynamic equilibrium and to detect conformational changes not directly observable with other methods. Dextran is comprised of a chain of pyranose rings that each undergoes an Angstrom-scale transition from a chair to boat conformation under a stretching force. Our analysis of the variance of the molecule's fluctuations verifies equilibrium throughout the force-extension curve, consistent with the expected thermodynamic ensemble. This validates further analysis of the variance in the transition region, which reveals an intermediate conformation between the chair and the boat on the sub-Angstrom scale. Our test of thermal equilibrium as well as our variance analysis can be readily extended to a wide variety of molecules, including proteins.

Elastic and dissipative properties of granular assemblies under uniaxial compression are studied both experimentally and by numerical simulations. Following a novel compaction procedure at varying oscillatory pressures, the stress response to a step strain reveals an exponential relaxation followed by a slow logarithmic decay. Simulations indicate that the latter arises from the coupling between damping and collective grain motion predominantly through sliding. We characterize an analogous "glass transition" for packed grains, below which the system shows aging in time-dependent sliding correlation functions.

The slow dynamics of granular flow is studied as an extension of static granular problems, which, as a consequence of shaking or related regimes, can be studied by the methods of statistical mechanics. For packed (i.e. 'jammed'), hard and rough objects, kinetic energy is a minor and ignorable quantity, as is strain. Hence, in the static case, the stress equations need supplementing by 'missing equations' depending solely on configurations. These are in the literature; this paper extends the equilibrium studies to slow dynamics, claiming that the strain rate (which is a consequence of flow, not of elastic strain) takes the place of stress, and as before, the analogue of Stokes's equation has to be supplemented by new 'missing equations' which are derived and which depend only on configurations.

In particulate materials, such as emulsions and granular media, a "jammed" system results if particles are packed together so that all particles are touching their neighbours, provided the density is sufficiently high. This paper studies through experiment, theory and simulation, the forces that particles exert upon one another in such a jammed state. Confocal microscopy of a compressed polydisperse emulsion provides a direct 3D measurement of the dispersed phase morphology within the bulk of the sample. This allows the determination of the probability distribution of interdroplet forces, P(f) where f is the magnitude of the force, from local droplet deformations. In parallel, the simplest form of the Boltzmann equation for the probability of force distributions predicts P(f) to be of the form e(-f/p), where p is proportional to the mean force f for large forces. This result is in good agreement with experimental and simulated data.