Previously, it has been reported that human telomeric DNA sequences could adopt in different experimental conditions four different intramolecular G-quadruplexes each involving three G-tetrad layers, namely Na + -solution antiparallel-stranded basket form, K + -crystal parallel-stranded propeller form, K + -solution (3+1) Form 1 and K + -solution (3+1) Form 2. Here we present a new intramolecular G-quadruplex adopted by a four-repeat human telomeric sequence in K + solution (Form 3). This structure is a basket-type G-quadruplex with only two G-tetrad layers: loops are successively edgewise, diagonal and edgewise; glycosidic conformations of guanines are syn•syn•anti•anti around each tetrad; each strand of the core has both a parallel and an antiparallel adjacent strands; there are one narrow, one wide and two medium grooves. Despite the presence of only two G-tetrads in the core, this structure is more stable than the three-G-tetrad intramolecular G-quadruplexes previously observed for human telomeric sequences in K + solution. Detailed structural elucidation of Form 3 revealed extensive base pairing and stacking in the loops capping both ends of the G-tetrad core, which might explain the high stability of the structure. This novel structure highlights the conformational heterogeneity of human telomeric DNA. It revealed a new folding principle for Gquadruplexes and suggests new loop sequences and structures for targeting in human telomeric DNA.

Recently, porous hydrophobic/oleophilic materials (PHOMs) have been shown to be the most promising candidates for cleaning up oil spills; however, due to their limited absorption capacity, a large quantity of PHOMs would be consumed in oil spill remediation, causing serious economic problems. In addition, the complicated and time-consuming process of oil recovery from these sorbents is also an obstacle to their practical application. To solve the above problems, we apply external pumping on PHOMs to realize the continuous collection of oil spills in situ from the water surface with high speed and efficiency. Based on this novel design, oil/water separation and oil collection can be simultaneously achieved in the remediation of oil spills, and the oil sorption capacity is no longer limited to the volume and weight of the sorption material. This novel external pumping technique may bring PHOMs a step closer to practical application in oil spill remediation.

Droplet jumping from condensing surfaces induced by droplet coalescence during dropwise condensation of mixed steam on a superhydrophobic surface can significantly enhance condensation heat transfer of mixed steam with non-condensable gas. This phenomenon was visually observed and theoretically analyzed in the present paper. The dynamic evolution of droplet and the velocity distribution inside the droplet during coalescence were simulated using multiphase lattice Boltzmann method. The energy distribution released by droplet coalescence was calculated statistically, and the jumping height induced by droplet coalescence on a superhydrophobic surface was predicted based on the energy conservation method. The theoretical predictions obtained by the modified model proposed in this paper agree well with the experimental observations.

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Abnormal aggregation of islet amyloid polypeptide (IAPP)into amyloid fibrils is a hallmark of type 2 diabetes. In this study, we investigated the initial oligomerization and subsequent addition of monomers to growing aggregates of human IAPP at the residue-specific level using NMR, atomic force microscopy, mass spectroscopy, and computational simulations. We found that in solution IAPPs rapidly associate into transient low-order oligomers such as dimers and trimers via interactions between histidine 18 and tyrosine 37. This initial event is proceeded by slow aggregation into higher-order spherical oligomers and elongated fibrils. In these two morphologically distinct types of aggregates IAPPs adopt structures with markedly different residual flexibility. Here we show that the anti-amyloidogenic compound resveratrol inhibits oligomerization and amyloid formation via binding to histidine 18, supporting the finding that this residue is crucial for on-pathway oligomer formation.

Nanostructured superhydrophobic surfaces have been actively explored to promote favorable droplet dynamics for a wide range of technological applications. However, the tendency of condensed droplets to form as pinned states greatly limits their applicability in enhancing condensation heat transfer efficiency. Despite recent progresses, the understanding of physical mechanisms governing the wetting transition of condensed droplets is still lacking. In this work, a nanostructured superhydrophobic surface with tapered nanogaps is fabricated to demonstrate the coordination of surface wetting property, topography, and the condensing condition on the wetting state and dynamic behavior of condensed droplets. Combining the environmental scanning electron microscopy and optical visualization methods, we systematically show the morphology of nucleated droplets in nanostructures and the droplet dynamic evolution throughout the growth stages, which provides the direct evidence of condensing condition-induced droplet wetting transition. When the surface subcooling is smaller than 0.3 K, the droplets formed as the Cassie-Baxter state, followed by coalescence-induced droplet jumping. With the increase of surface subcooling up to 0.6 K, however, droplet formation occurs randomly inside nanogaps, resulting in the loss of superhydrophobicity. These new observations along with the new insights about the coordination of surface properties and condensing conditions on droplet wetting transition are useful for guiding the development of novel surfaces for improving droplet removal and phase-change heat transfer.

Aggregation of the amyloid β protein (Aβ) peptide with 40 or 42 residues is one key feature in Alzheimer's disease (AD). The 1,4-naphthoquinon-2-yl-L-tryptophan (NQTrp) molecule was reported to alter Aβ self-assembly and reduce toxicity. Though nuclear magnetic resonance experiments and various simulations provided atomic information about the interaction of NQTrp with Aβ peptides spanning the regions of residues 12−28 and 17−42, none of these studies were conducted on the fulllength Aβ1−42 peptide. To this end, we performed extensive atomistic replica exchange molecular dynamics simulations of Aβ1−42 dimer with two NQTrp molecules in explicit solvent, by using a force field known to fold diverse proteins correctly. The interactions between NQTrp and Aβ1−42, which change the Aβ interface by reducing most of the intermolecular contacts, are found to be very dynamic and multiple, leading to many transient binding sites. The most favorable binding residues are Arg5, Asp7, Tyr10, His13, Lys16, Lys18, Phe19/Phe20, and Leu34/Met35, providing therefore a completely different picture from in vitro and in silico experiments with NQTrp with shorter Aβ fragments. Importantly, the 10 hot residues that we identified explain the beneficial effect of NQTrp in reducing both the level of Aβ1−42 aggregation and toxicity. Our results also indicate that there is room to design more efficient drugs targeting Aβ1−42 dimer against AD.

In the cell, protein complexes form by relying on specific interactions between their monomers. Excluded volume effects due to molecular crowding would lead to correlations between molecules even without specific interactions. What is the interplay of these effects in the crowded cellular environment? We study dimerization of a model homodimer when the mondimers are free and when they are tethered to each other. We consider a structured environment: Two monomers first diffuse into a cavity of size L and then fold and bind within the cavity. The folding and binding are simulated by using molecular dynamics based on a simplified topology based model. The confinement in the cell is described by an effective molecular concentration C ϳ L ؊3 . A two-state coupled folding and binding behavior is found. We show the maximal rate of dimerization occurred at an effective molecular concentration C op Ӎ 1 mM, which is a relevant cellular concentration. In contrast, for tethered chains the rate keeps at a plateau when C < C op but then decreases sharply when C > C op . For both the free and tethered cases, the simulated variation of the rate of dimerization and thermodynamic stability with effective molecular concentration agrees well with experimental observations. In addition, a theoretical argument for the effects of confinement on dimerization is also made. molecular crowding ͉ folding and binding ͉ effective molecular concentration ͉ Arc homodimer monolayer ͉ native topology-based models