SearcharxivSearch

arXiv · 2107.13836

Fold analysis of crumpled sheet using micro computed tomography

Abstract

Hand crumpled paper balls involve intricate structure with a network of creases and vertices, yet show simple scaling properties, which suggests self-similarity of the structure. We investigate the internal structure of crumpled papers by the micro computed tomography (micro-CT) without destroying or unfolding them. From the reconstructed three dimensional data, we examine several power laws for the crumpled square sheets of paper of the sizes $L=50\sim 300$ mm, and obtain the mass fractal dimension $D_M = 2.7\pm 0.1$ by the relation between the mass and the radius of gyration of the balls, and the fractal dimension $2.5\lesssim d_f \lesssim 2.8$ for the internal structure of each crumpled paper ball by the box counting method in the real space and the structure factors in the Fourier space; The data for the paper sheets are consistent with $D_M = d_f$, suggesting that the self-similarity in the structure of each crumpled ball gives rise to the similarity among the balls with different sizes. We also examine the cellophane sheets and the aluminium foils of the size $L=200$ mm and obtain $2.6\lesssim d_f\lesssim 2.8$ for both of them. The micro-CT also allows us to reconstruct 3-d structure of a line drawn on the crumpled sheets of paper. The Hurst exponent for the root mean square displacement along the line is estimated as $H\approx 0.9$ for the length scale shorter than the scale of the radius of gyration, beyond which the line structure becomes more random with $H\sim 0.5$.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Yumino Hayase, Hitoshi Aonuma, Satoshi Takahara, Takahiro Sakaue, Shun'ichi Kaneko, Hiizu Nakanishi. 2021-07-29. Fold analysis of crumpled sheet using micro computed tomography. https://arxiv.org/abs/2107.13836

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related papers

Slow Dynamics and the Geometry of Jammed Packings

Saddle points in the energy landscape of granular packings dominate the discrete steepest descent dynamics and ultimately determine the path that an out of mechanical equilibrium packing will follow and the resulting stable minimum that it will find. The saddle points that ultimately determine the resulting minima tend to be low-index saddle points. For models with an analytic energy landscape, such as the $p$-spin model, the steepest descent minimization path is affected by higher-index saddle points, which pull the system towards saddle points of decreasing index before arriving at the minima. Here, we examine the steepest descent minimization path of granular packings and compare them to the $p$-spin model. We show that the granular packing steepest descent minimization paths act like their smooth energy landscape counterparts and get attracted by saddle points. The index versus time curves for all models follow a shifted, stretched exponential. We further show that the shape parameter for the granular packings is unchanged when the energy landscape is modified to become analytic (Gaussian potential in a harmonic well) or non-local (Mari-Krzakala-Kurchan). The $p$-spin, on the other hand, has a significantly larger shape parameter. The reason is not due to the dimensionality, packing fraction, nonanalyticity, or the locality of the Hamiltonian of the models. The exact reason for the discrepancy in the shape parameter is \st{still} an unsolved mystery.

cond-mat.soft

A Phase-Field Study of Desiccation Crack Pattern Maturation under Drying-Wetting Cycles

The characteristic intersection angle of the desiccation crack relaxes from near \ang{90} toward \ang{120} under repeated drying--wetting cycles. However, the theoretical understanding of this relaxation is insufficient, especially the modeling of the drying--wetting cycles. Here we introduce a phase-field model of desiccation fracture, extending the model proposed in previous studies by adding crack healing and a scar effect left by past cracks. By repeating drying--wetting cycles in a finite element simulation, we find that the angle distribution develops a growing peak near \ang{120} as the cycle number increases, consistent with experiments. The standard deviation of the intersection angle from \ang{120} relaxes exponentially with a characteristic time of about 2.85 cycles. These results are consistent with experiments, except that the characteristic time is slightly smaller than the experimental value. Crack energy dominates the total energy and also relaxes exponentially with nearly the same characteristic cycle as the angle relaxation. This decay is driven mainly by a shortening of the effective crack length rather than a change in effective fracture toughness.

cond-mat.soft

Kinetics of ferritin crystal formation and melting in acoustically levitated droplets

Understanding protein crystallization pathways is essential for controlling crystallization in structural biology, materials science, and pharmaceutical applications. Classical nucleation theory does not fully capture crystallization processes for several proteins, including ferritin. Here, we combine acoustic levitation with small- and wide-angle X-ray scattering (SAXS and WAXS) to monitor ferritin crystallization in evaporating aqueous polyethylene glycol (PEG) solutions. Acoustic levitation rapidly drives the droplets through a broad range of protein and polymer concentrations, enabling time-resolved measurements of crystallization during evaporation. The scattering data show that ferritin crystals form during evaporation and subsequently lose their crystalline order upon further dehydration. Varying the PEG molecular weight switches between distinct crystallization pathways: one dominated by attractive protein-protein interactions and another dominated by repulsive interactions and excluded-volume effects. Furthermore, we find that lower molecular weight PEG (1000 g/mol) suppresses the dehydration-induced loss of crystalline order observed for higher molecular weight PEG (6000 g/mol), providing a simple strategy for improving protein crystal stability.

cond-mat.soft