Publications by authors named "John D Treado"

The spongy mesophyll is a complex, porous tissue found in plant leaves that enables carbon capture and provides mechanical stability. Unlike many other biological tissues, which remain confluent throughout development, the spongy mesophyll must develop from an initially confluent tissue into a tortuous network of cells with a large proportion of intercellular airspace. How the airspace in the spongy mesophyll develops while the tissue remains mechanically stable is unknown.

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Numerous experimental and computational studies show that continuous hopper flows of granular materials obey the Beverloo equation that relates the volume flow rate and the orifice width : ∼ (/ - ), where is the average particle diameter, is an offset where ∼ 0, the power-law scaling exponent = - 1/2, and is the spatial dimension. Recent studies of hopper flows of deformable particles in different background fluids suggest that the particle stiffness and dissipation mechanism can also strongly affect the power-law scaling exponent . We carry out computational studies of hopper flows of deformable particles with both kinetic friction and background fluid dissipation in two and three dimensions.

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Correction for 'The structural, vibrational, and mechanical properties of jammed packings of deformable particles in three dimensions' by Dong Wang , , 2021, , 9901-9915, DOI: 10.1039/D1SM01228B.

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We investigate the structural, vibrational, and mechanical properties of jammed packings of deformable particles with shape degrees of freedom in three dimensions (3D). Each 3D deformable particle is modeled as a surface-triangulated polyhedron, with spherical vertices whose positions are determined by a shape-energy function with terms that constrain the particle surface area, volume, and curvature, and prevent interparticle overlap. We show that jammed packings of deformable particles without bending energy possess low-frequency, quartic vibrational modes, whose number decreases with increasing asphericity and matches the number of missing contacts relative to the isostatic value.

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Article Synopsis
  • The challenge of distinguishing real protein structures from computational model decoys remains unresolved, requiring an understanding of key physical features that characterize authentic proteins.
  • Two datasets were utilized for comparison: one from a protein structure prediction competition and another generated by a tool that creates decoys with varying deviations from actual structures.
  • The study found that decoys often have inconsistencies in features like core density, residue distribution, and hydrophobicity, leading to the development of a neural network model that effectively ranks these decoys based on crucial protein characteristics.
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There have been several studies suggesting that protein structures solved by NMR spectroscopy and X-ray crystallography show significant differences. To understand the origin of these differences, we assembled a database of high-quality protein structures solved by both methods. We also find significant differences between NMR and crystal structures-in the root-mean-square deviations of the C atomic positions, identities of core amino acids, backbone, and side-chain dihedral angles, and packing fraction of core residues.

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Dense packing of hydrophobic residues in the cores of globular proteins determines their stability. Recently, we have shown that protein cores possess packing fraction ϕ≈0.56, which is the same as dense, random packing of amino-acid-shaped particles.

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We present the structure of an engineered protein-protein interface between two beta barrel proteins, which is mediated by interactions between threonine (Thr) residues. This Thr zipper structure suggests that the protein interface is stabilized by close-packing of the Thr residues, with only one intermonomer hydrogen bond (H-bond) between two of the Thr residues. This Thr-rich interface provides a unique opportunity to study the behavior of Thr in the context of many other Thr residues.

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