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MCrAlY bond coats are widely used as oxidation resistant coatings on superalloys. The major phase is the thermally stable intermetallic β–NiAl phase. The addition of Cr increases the oxidation and corrosion resistance, but leads to the formation of α–Cr precipitates. Both phases are brittle and limit the fracture toughness of these coatings. In order to study the influence of thermal exposure and the resulting changing chemical composition on the fracture properties, the fracture toughness of both phases was measured by notched micro-cantilever bending, after the processing and after oxidation by thermal cycling. The fracture toughness of β–NiAl decreased during thermal cycling due to the depletion in Al, whereas the fracture toughness and the composition of α–Cr stayed constant. Since the fracture toughness of α–Cr was lower compared to β–NiAl, the formation of α–Cr precipitates is supposed to decrease the fracture toughness of the bond coat.

Yttria stabilized tetragonal zirconia polycrystal (Y-TZP) owes its high toughness to transformation toughening, a mechanism that requires the development of a process zone. It is important to measure if and to what extent the size of components can be reduced. In this study, tests were carried out using focused ion beam or picosecond milled pre-notched, 3 mol percent Y2O3 (3Y-) TZP micro-cantilever (10–250 μm) beams. The tests show clearly that the maximum fracture resistance is size dependent and the plateau toughness was not reached in any of the small-scale samples. A correlation between transformability of the tetragonal phase and the measured fracture resistance became visible only for the largest micro cantilever but did not reach the values measured in macroscopic samples. Based on these results, it is not advantageous to use very tough zirconia materials in components with dimensions smaller than ∼0.25 mm, as the high toughness is not fully realized.

Bond coats are essential in gas turbine technology for oxidation protection. Freestanding MCrAlY (M = Ni, Co) bond coats were investigated with respect to their creep strength at elevated temperatures. Three types of MCrAlY, a Ni-based bond coat Amdry 386, a Co-based bond coat Amdry 9954 and Amdry 9954 + 2 wt% Al2O3 (ODS = oxide dispersion strengthened) produced by low pressure plasma spraying, were analyzed. The two phase microstructure of the bond coats consists of a fcc γ-Ni solid solution and a B2 β-NiAl phase. Constant load experiments were performed in a thermomechanical analyzer at temperatures between 900 and 950 °C. Microtensile test specimens with a diameter of 450 µm were produced by a high-precision grinding and polishing process. Creep rupture was mainly due to void nucleation along the β–γ interfaces and grain boundaries. The time to failure is larger in Ni-based Amdry 386 compared to that in Co-based Amdry 9954 due to a higher fraction of the high-strength β-NiAl phase at test temperatures. The addition of ODS-particles in the Co-based bond coat Amdry 9954 resulted in a better creep resistance but lower ductility in comparison to ODS-particle-free Amdry 9954.

The crack susceptibility during processing has a crucial influence on the workability of wrought alloys. In particular, the processing of high-strength alloys that are prone to cracking is challenging and various process parameters have to be optimized to achieve a good formability. The polycrystalline CoNi-base superalloy CoWAlloy1 provides a high potential for high-temperature applications due to it having a large forging window, a high γ′ fraction and excellent creep properties. In order to study its formability during hot rolling, its deformation behavior and susceptibility to cracking were characterized by sub- and supersolvus compression tests at temperatures between 1000–1150 °C. At temperatures around the γ′ solvus temperature, no cracks formed during the compression testing, while at lower temperatures, cracking occurred. Additionally, an in-situ high-temperature small-angle neutron scattering revealed the phase fractions and the precipitate size distributions at different processing temperatures. It was found that a high fraction of γ′ forms during cooling and cracking starts at the surface of the bar, when the hot bar encounters the cold rolls during hot rolling. Apparently, the precipitation of γ′, which causes a high strength and reduced ductility, and the absent recrystallization leads to pronounced crack propagation and limited formability below the γ′ solvus temperature.

The effects of N-terminal acetylation of the high molecular weight tropomyosin isoforms Tpm1.6 and Tpm2.1 and the low molecular weight isoforms Tpm1.12, Tpm3.1, and Tpm4.2 on the actin affinity and the thermal stability of actin-tropomyosin cofilaments are described. Furthermore, we show how the exchange of cytoskeletal tropomyosin isoforms and their N-terminal acetylation affects the kinetic and chemomechanical properties of cytoskeletal actin-tropomyosin-myosin complexes. Our results reveal the extent to which the different actin-tropomyosin-myosin complexes differ in their kinetic and functional properties. The maximum sliding velocity of the actin filament as well as the optimal motor density for continuous unidirectional movement, parameters that were previously considered to be unique and invariant properties of each myosin isoform, are shown to be influenced by the exchange of the tropomyosin isoform and the N-terminal acetylation of tropomyosin.

Mass spectrometry-based proteomics provides a holistic snapshot of the entire protein set of a living cell on a molecular level. Currently, only a few deep learning approaches that involve peptide fragmentation spectra, which represent partial sequence information of proteins, exist. Commonly, these approaches lack the ability to characterize less studied or even unknown patterns in spectra because of their use of explicit domain knowledge. To elevate unrestricted learning from spectra, we introduce AHLF, a deep learning model that is end-to-end trained on 19.2 million spectra from multiple phosphoproteomic data sets. AHLF is interpretable and we show that peak-level feature importances and pairwise interactions between peaks are in line with corresponding peptide fragments. We demonstrate our approach by detecting post-translational modifications, specifically protein phosphorylation based on only the fragmentation spectrum without a database search. AHLF increases the area under the receiver operating characteristic curve (AUC) by an average of 9.4% on recent phosphoproteomic data compared to the current-state-of-the-art on this task. To show the broad applicability of AHLF we use transfer learning to also detect cross-linked peptides, as used in protein structure analysis, with an AUC of up to 94%. We expect our approach to directly apply to cell signaling and structural biology which use phosphoproteomic and cross-linking data, but in principal any mass spectrometry based study can benefit from an interpretable, end-to-end trained model like AHLF.Availabilityhttps://gitlab.com/dacs-hpi/ahlfContactbernhard.renard@hpi.de

Filamentous fungi belonging to the genus Fusarium are notorious plant-pathogens that infect, damage and contaminate a wide variety of important crops. Phenamacril is the first member of a novel class of single-site acting cyanoacrylate fungicides which has proven highly effective against important members of the genus Fusarium. However, the recent emergence of field-resistant strains exhibiting qualitative resistance poses a major obstacle for the continued use of phenamacril. In this study, we synthesized novel cyanoacrylate compounds based on the phenamacril-scaffold to test their growth-inhibitory potential against wild-type Fusarium and phenamacril-resistant strains. Our findings show that most chemical modifications to the phenamacril-scaffold are associated with almost complete loss of fungicidal activity and in vitro inhibition of myosin motor domain ATPase activity.

The MYO1C gene produces three alternatively spliced isoforms, differing only in their N-terminal regions (NTRs). These isoforms, which exhibit both specific and overlapping nuclear and cytoplasmic functions, have different expression levels and nuclear–cytoplasmic partitioning. To investigate the effect of NTR extensions on the enzymatic behavior of individual isoforms, we overexpressed and purified the three full-length human isoforms from suspension-adapted HEK cells. MYO1CC favored the actomyosin closed state (AMC), MYO1C16 populated the actomyosin open state (AMO) and AMC equally, and MYO1C35 favored the AMO state. Moreover, the full-length constructs isomerized before ADP release, which has not been observed previously in truncated MYO1CC constructs. Furthermore, global numerical simulation analysis predicted that MYO1C35 populated the actomyosin·ADP closed state (AMDC) 5-fold more than the actomyosin·ADP open state (AMDO) and to a greater degree than MYO1CC and MYO1C16 (4- and 2-fold, respectively). On the basis of a homology model of the 35-amino acid NTR of MYO1C35 (NTR35) docked to the X-ray structure of MYO1CC, we predicted that MYO1C35 NTR residue Arg-21 would engage in a specific interaction with post-relay helix residue Glu-469, which affects the mechanics of the myosin power stroke. In addition, we found that adding the NTR35 peptide to MYO1CC yielded a protein that transiently mimics MYO1C35 kinetic behavior. By contrast, NTR35, which harbors the R21G mutation, was unable to confer MYO1C35-like kinetic behavior. Thus, the NTRs affect the specific nucleotide-binding properties of MYO1C isoforms, adding to their kinetic diversity. We propose that this level of fine-tuning within MYO1C broadens its adaptability within cells.

This paper presents the high temperature yield and fatigue strength as well as thermophysical properties of two polycrystalline wrought γ/γ′ Co-base superalloys developed for application in a temperature regime above 700 °C. The alloys CoWAlloy1 (Co42Ni32Cr12Al6W3Ti2.5Ta1.5 + Si,C,B,Zr,Hf) and CoWAlloy2 (Co41Ni32Cr12Al9W5 + Ti,Ta,Si,C,B,Zr,Hf) exhibited solidus temperatures of 1070 °C and 1030 °C, respectively, and a γ′ fraction of about 50%. CoWAlloy2 displayed a rather high Young’s modulus of 250 GPa. The two Co-base superalloys showed a good high temperature strength exceeding Ni-base disc alloys U720Li and Waspaloy at temperatures above 800 °C. When comparing the yield strength from tensile and compression tests, no asymmetry could be found. The low-cycle fatigue life of CoWAlloy2 at a total strain amplitude of 0.5% is similar to that of U720Li and Waspaloy (about 370 cycles, R = −1). During long-term aging for 1024 h at 750 °C, no additional phases were formed and the room temperature hardness barely changed.

PDF of https://doi.org/10.1002/adem.202001464 Lamellar eutectic NiAl–Cr(Mo) alloys show an increased fracture toughness due to different toughening mechanisms. These mechanisms result from the fibrous or lamellar microstructure of the two constituting phases α‐Cr(Mo) and β‐NiAl. However, the fracture toughness of the individual phases and the evolution from early crack growth to the toughening mechanisms have not yet been systematically studied. Herein, bending tests on focused ion beam (FIB)‐notched microcantilever beams are used to characterize the small‐scale fracture properties. The micromechanical investigations reveal that the fracture toughness of the α‐Cr(Mo) phase (7.5−9.1 MPa𝑚⎯⎯⎯√7.5−9.1 MPam) is much higher than the fracture toughness of β‐NiAl (2.2−2.9 MPa𝑚⎯⎯⎯√2.2−2.9 MPam). Larger cantilevers in the crack arresting orientation show an enhanced fracture toughness with up to14.4 MPa𝑚⎯⎯⎯√14.4 MPam, which is still lower than the one of macroscopic experiments. This is attributed to the small interaction volume of the crack, which hinders the full exploitation of potential extrinsic toughening mechanisms.

The cyanoacrylate compound phenamacril (also known as JS399–19) is a recently identified fungicide that exerts its antifungal effect on susceptible Fusarium species by inhibiting the ATPase activity of their myosin class I motor domains. Although much is known about the antifungal spectrum of phenamacril, the exact mechanism behind the phenamacril-mediated inhibition remains to be resolved. Here, we describe the characterization of the effect of phenamacril on purified myosin motor constructs from the model plant pathogen and phenamacril-susceptible species Fusarium graminearum, phenamacril-resistant Fusarium species, and the mycetozoan model organism Dictyostelium discoideum. Our results show that phenamacril potently (IC(50) ∼360 nm), reversibly, and noncompetitively inhibits ATP turnover, actin binding during ATP turnover, and motor activity of F. graminearum myosin-1. Phenamacril also inhibits the ATPase activity of Fusarium avenaceum myosin-1 but has little or no inhibitory effect on the motor activity of Fusarium solani myosin-1, human myosin-1c, and D. discoideum myosin isoforms 1B, 1E, and 2. Our findings indicate that phenamacril is a species-specific, noncompetitive inhibitor of class I myosin in susceptible Fusarium sp.

The MYO1C gene produces three alternatively spliced isoforms, differing only in their N-terminal regions (NTRs). These isoforms, which exhibit both specific and overlapping nuclear and cytoplasmic functions, have different expression levels and nuclear–cytoplasmic partitioning. To investigate the effect of NTR extensions on the enzymatic behavior of individual isoforms, we overexpressed and purified the three full-length human isoforms from suspension-adapted HEK cells. MYO1CC favored the actomyosin closed state (AMC), MYO1C16 populated the actomyosin open state (AMO) and AMC equally, and MYO1C35 favored the AMO state. Moreover, the full-length constructs isomerized before ADP release, which has not been observed previously in truncated MYO1CC constructs. Furthermore, global numerical simulation analysis predicted that MYO1C35 populated the actomyosin·ADP closed state (AMDC) 5-fold more than the actomyosin·ADP open state (AMDO) and to a greater degree than MYO1CC and MYO1C16 (4- and 2-fold, respectively). On the basis of a homology model of the 35-amino acid NTR of MYO1C35 (NTR35) docked to the X-ray structure of MYO1CC, we predicted that MYO1C35 NTR residue Arg-21 would engage in a specific interaction with post-relay helix residue Glu-469, which affects the mechanics of the myosin power stroke. In addition, we found that adding the NTR35 peptide to MYO1CC yielded a protein that transiently mimics MYO1C35 kinetic behavior. By contrast, NTR35, which harbors the R21G mutation, was unable to confer MYO1C35-like kinetic behavior. Thus, the NTRs affect the specific nucleotide-binding properties of MYO1C isoforms, adding to their kinetic diversity. We propose that this level of fine-tuning within MYO1C broadens its adaptability within cells.

The mechanical properties of low-pressure plasma sprayed (LPPS) MCrAlY (M = Ni, Co) bond coats, Amdry 386, Amdry 9954 and oxide dispersion strengthened (ODS) Amdry 9954 (named Amdry 9954 + ODS) were investigated after annealing in three atmospheres: Ar&ndash, O2, Ar&ndash, H2O, and Ar&ndash, H2&ndash, H2O. Freestanding bond coats were investigated to avoid any influence from the substrate. Miniaturized cylindrical tensile specimens were produced by a special grinding process and then tested in a thermomechanical analyzer (TMA) within a temperature range of 900&ndash, 950 &deg, C. Grain size and phase fraction of all bond coats were investigated by EBSD before testing and no difference in microstructure was revealed due to annealing in various atmospheres. The influence of annealing in different atmospheres on the creep strength was not very pronounced for the Co-based bond coats Amdry 9954 and Amdry 9954 + ODS in the tested conditions. The ODS bond coats revealed significantly higher creep strength but a lower strain to failure than the ODS-free Amdry 9954. The Ni-based bond coat Amdry 386 showed higher creep strength than Amdry 9954 due to the higher fraction of the &beta, NiAl phase. Additionally, its creep properties at 900 &deg, C were much more affected by annealing in different atmospheres. The bond coat Amdry 386 annealed in an Ar&ndash, H2O atmosphere showed a significantly lower creep rate than the bond coat annealed in Ar&ndash, O2 and Ar&ndash, H2O atmospheres.

Fungicide application remains a vital component in the management of Fusarium-induced plant infections, but environmental concerns and resistance toward some of the commonly used fungicides has spurred efforts into developing new specific fungicides. Phenamacril, a cyanoacrylate fungicide, represents a novel class of seemingly Fusarium-specific and environmentally benign fungicides that could hold great potential in our future efforts toward minimizing the occurrence and severity of Fusarium-induced plant infections. Phenamacril targets the motor domain of Fusarium class I myosin [1-2], an ubiquitous molecular motor which facilitates numerous ATP-driven and actin-associated processes within the cell. The myosin superfamiliy is divided into approximately 20 different classes (classes I, II, V and XVII are present in fungi), each potentially having several isoforms. While the taskspecific C-terminal tail domains are highly variable in size and function, the N-terminal motor domains remain highly conservered, both structurally and functionally. Interestingly, Phenamacril-resistance has been shown to correlate with single amino acid mutations in a highly conserved region of the motor domain [1], a region involved in the allosteric communication between the actin- and nucleotide binding-site [3]. To gain further insight into the specificity, the inhibitory potential and nature of the Phenamacril-mediated inhibitionof Fusarium myosin, we overexpressed Fusarium class I myosins in Sf9 insect cells. Through a combination of NADH-coupled and in vitro motility assays, we demonstrated that Phenamacril is a very potent but functionally reversible inhibitor of Fusarium class I myosin. Similarly, we demonstrated that Phenamacril had no or only minimal inhibitory effect on human myosin 1c, Dictyostelium discoideum class I and II myosins, but that the motor domain of the Phenamacril-resistant F. solani f. sp. pisi was highly inhibited by Phenamacril in vitro. This suggests thatdespite of the high degree of structural conservation in the myosin super-family, subtle differences render Phenamacril a highly specific and potent reversible inhibitor of Fusarium class I myosin.[1] Zheng Z, Yiping H, Yiqiang C et al (2015): Sci Rep, 5 (2021): 8248.[2] Zhang C, Yun C, Yanni Y et al (2015): Environ Microbiol, 17 (8): 2735–46.[3] Krishna C, Taft MH, Martin R et al (2011): J Biol Chem, 286 (34): 29700–708.