Journal: ACS Central Science

Article Title: Programmable Light-Driven Color Tuning of Perovskite Quantum Dots

doi: 10.1021/acscentsci.5c01651

Figure Lengend Snippet: (A,B) Time-resolved evolution of λ em during UV-on and UV-off experiments for blue- and red-shifts, respectively. The gray-shaded regions represent UV-off intervals. FSDL’s PIAER reproducibility study with random sampling experiments for (C, blue) chloride- (D, red) and iodide-exchange reactions. Each plot shows fwhm, P PLQY , and λ em across 10 experiments with 5 repeats of the same baseline (black data points) and randomly selected (blue and red data points) PIAER conditions. Black dashed lines indicate the mean values across baseline condition replicates. Experimental conditions (baseline): [CsPbBr 3 ] = 4.2 μM; [DCM] = 4.1 M; [1-iodopropane] = 0.24 M; photon flux = 15 pmol s –1 (DCM) and 55 pmol s –1 (1-iodopropane); residence time = 2.0 min; T = 23 °C.

Article Snippet: This normalization corrects for variations in NCs concentration and excitation efficiency, ensuring that the metric reflects the fraction of absorbed photons re-emitted rather than raw PL I . , , We validated the FSDL’s in situ characterization module by benchmarking it against conventional benchtop spectroscopy (FS5, Edinburgh Instruments).

Techniques: Sampling

Journal: ACS Central Science

Article Title: Programmable Light-Driven Color Tuning of Perovskite Quantum Dots

doi: 10.1021/acscentsci.5c01651

Figure Lengend Snippet: Schematic overview of the closed-loop autonomous experimentation framework for programmable synthesis of high-performing MHP NCs via PIAERs. The multiobjective BO loop is initiated by an LHS strategy to generate a diverse and unbiased set of initial experiments for training the surrogate ML model. These experiments are executed using a single-droplet microfluidic photoreactor. In situ optical characterization captures the resulting UV/vis absorption and PL spectra, from which key photophysical metrics are extracted via automated data processing. The surrogate ML model, based on Gaussian Process regression (GPR), is then retrained with the newly acquired data, updating its predictions and uncertainty estimates over the high-dimensional parameter space. Sampling strategies guided by acquisition functions (e.g., Expected Hypervolume Improvement) are used to explore the updated surrogate landscape and identify promising regions near the Pareto front. A decision policy selects the next experiment by balancing exploration and exploitation, leading to the generation of new input conditions that are passed to the FSDL’s hardware for execution. This iterative loop continues until convergence on optimal PIAER conditions for targeted optical outputs, enabling on-demand, material-efficient synthesis of compositionally tuned MHP NCs.

Article Snippet: This normalization corrects for variations in NCs concentration and excitation efficiency, ensuring that the metric reflects the fraction of absorbed photons re-emitted rather than raw PL I . , , We validated the FSDL’s in situ characterization module by benchmarking it against conventional benchtop spectroscopy (FS5, Edinburgh Instruments).

Techniques: In Situ, Sampling

Journal: Frontiers in Plant Science

Article Title: A new member of the psToc159 family contributes to distinct protein targeting pathways in pea chloroplasts

doi: 10.3389/fpls.2014.00239

Figure Lengend Snippet: Energy dependence of FSD1 import . In vitro import assays into pea chloroplasts are depicted. Lane 1 shows 10% of translation product. All samples were treated with thermolysin after import (lanes 2–6). ATP-concentrations in mM are indicated on top of the panel. Representative results from n = 3 independent experiments are depicted.

Article Snippet: Outer envelope membranes were prepared from pea chloroplasts according to Cline et al. ( ) and incubated with a synthetic peptide representing the N-terminal region of FSD1 (amino acids 1–25) carrying a C-terminal biotin-moiety (JPT Peptide Technologies GmbH, Berlin, Germany) in the presence of 0.1 mM ATP at 4°C for 5 min. After recovery of the membranes by centrifugation they were treated with 5 mM of N-(α-Maleimidoacetoxy) succinimide ester (AMAS, Thermo Fisher Scientific, Schwerte, Germany) for 30 min on ice to initiate cross-linking.

Techniques: In Vitro

Journal: Frontiers in Plant Science

Article Title: A new member of the psToc159 family contributes to distinct protein targeting pathways in pea chloroplasts

doi: 10.3389/fpls.2014.00239

Figure Lengend Snippet: FSD1 import critically depends on protease sensitive surface receptors. (A) Immunoblot of chloroplasts used for import experiments before and after thermolysin pre-treatment. The membrane was probed for Tic110, Toc159, and Toc34. Representative results from n = 3 independent experiments are depicted. (B) In vitro import assays into pea chloroplasts are depicted. Lane 1 shows 10% of translation product. Thl-pre (+) indicates thermolysin digestion before the import reaction (lane 3). All samples were treated with thermolysin after import.

Article Snippet: Outer envelope membranes were prepared from pea chloroplasts according to Cline et al. ( ) and incubated with a synthetic peptide representing the N-terminal region of FSD1 (amino acids 1–25) carrying a C-terminal biotin-moiety (JPT Peptide Technologies GmbH, Berlin, Germany) in the presence of 0.1 mM ATP at 4°C for 5 min. After recovery of the membranes by centrifugation they were treated with 5 mM of N-(α-Maleimidoacetoxy) succinimide ester (AMAS, Thermo Fisher Scientific, Schwerte, Germany) for 30 min on ice to initiate cross-linking.

Techniques: Western Blot, Membrane, In Vitro

Journal: Frontiers in Plant Science

Article Title: A new member of the psToc159 family contributes to distinct protein targeting pathways in pea chloroplasts

doi: 10.3389/fpls.2014.00239

Figure Lengend Snippet: FSD1 import uses parts of the general import pathway. (A) In vitro import assays into pea chloroplasts are depicted. Lane 1 shows 10% of translation product. Increasing amounts of heterologously expressed pSSU as indicated on top of the panel were added to the import reaction. (B) Same as in (A) but with FSD1 as competitor. All samples were treated with thermolysin after import. Representative results from n = 3 independent experiments are depicted.

Article Snippet: Outer envelope membranes were prepared from pea chloroplasts according to Cline et al. ( ) and incubated with a synthetic peptide representing the N-terminal region of FSD1 (amino acids 1–25) carrying a C-terminal biotin-moiety (JPT Peptide Technologies GmbH, Berlin, Germany) in the presence of 0.1 mM ATP at 4°C for 5 min. After recovery of the membranes by centrifugation they were treated with 5 mM of N-(α-Maleimidoacetoxy) succinimide ester (AMAS, Thermo Fisher Scientific, Schwerte, Germany) for 30 min on ice to initiate cross-linking.

Techniques: In Vitro

Journal: Frontiers in Plant Science

Article Title: A new member of the psToc159 family contributes to distinct protein targeting pathways in pea chloroplasts

doi: 10.3389/fpls.2014.00239

Figure Lengend Snippet: FSD1 N-terminus interacts with large outer envelope proteins . A synthetic peptide representing the first 25 AA of FSD1 including a biotin moiety was incubated with outer envelope vesicles, chemically cross-linked and subjected to SDS-PAGE. The samples were analyzed by silver staining and western blot. A band not present in the control was analyzed by mass spectroscopy (indicated by an asterisk).

Article Snippet: Outer envelope membranes were prepared from pea chloroplasts according to Cline et al. ( ) and incubated with a synthetic peptide representing the N-terminal region of FSD1 (amino acids 1–25) carrying a C-terminal biotin-moiety (JPT Peptide Technologies GmbH, Berlin, Germany) in the presence of 0.1 mM ATP at 4°C for 5 min. After recovery of the membranes by centrifugation they were treated with 5 mM of N-(α-Maleimidoacetoxy) succinimide ester (AMAS, Thermo Fisher Scientific, Schwerte, Germany) for 30 min on ice to initiate cross-linking.

Techniques: Incubation, SDS Page, Silver Staining, Western Blot, Control, Mass Spectrometry

Journal: Frontiers in Plant Science

Article Title: A new member of the psToc159 family contributes to distinct protein targeting pathways in pea chloroplasts

doi: 10.3389/fpls.2014.00239

Figure Lengend Snippet: FSD1 import is inhibited in the presence of psToc120 A-domain . In vitro import assays into pea chloroplasts are depicted. Lane 1 shows 10% of translation product. Increasing concentrations of purified psToc120 A-domain were incubated with in vitro translated chloroplast proteins prior to import. All samples were treated with thermolysin after the reaction. Representative results from n = 3 independent experiments are depicted.

Article Snippet: Outer envelope membranes were prepared from pea chloroplasts according to Cline et al. ( ) and incubated with a synthetic peptide representing the N-terminal region of FSD1 (amino acids 1–25) carrying a C-terminal biotin-moiety (JPT Peptide Technologies GmbH, Berlin, Germany) in the presence of 0.1 mM ATP at 4°C for 5 min. After recovery of the membranes by centrifugation they were treated with 5 mM of N-(α-Maleimidoacetoxy) succinimide ester (AMAS, Thermo Fisher Scientific, Schwerte, Germany) for 30 min on ice to initiate cross-linking.

Techniques: In Vitro, Purification, Incubation

Journal: Frontiers in Plant Science

Article Title: A new member of the psToc159 family contributes to distinct protein targeting pathways in pea chloroplasts

doi: 10.3389/fpls.2014.00239

Figure Lengend Snippet: The extreme N-terminus of FSD1 is indispensable for import . In vitro import assays into pea chloroplasts are shown. Lane 1 represents 10% of translation product, Thl (+) indicates thermolysin digestion after the import reaction (lane 3). Please note the second band in the translation product of FSD1DN (indicated by an asterisk) which might derive from a downstream methionine recognized in the reticulocyte lysate as an alternative start. Representative results from n = 3 independent experiments are depicted.

Article Snippet: Outer envelope membranes were prepared from pea chloroplasts according to Cline et al. ( ) and incubated with a synthetic peptide representing the N-terminal region of FSD1 (amino acids 1–25) carrying a C-terminal biotin-moiety (JPT Peptide Technologies GmbH, Berlin, Germany) in the presence of 0.1 mM ATP at 4°C for 5 min. After recovery of the membranes by centrifugation they were treated with 5 mM of N-(α-Maleimidoacetoxy) succinimide ester (AMAS, Thermo Fisher Scientific, Schwerte, Germany) for 30 min on ice to initiate cross-linking.

Techniques: In Vitro

Journal: Frontiers in Plant Science

Article Title: A new member of the psToc159 family contributes to distinct protein targeting pathways in pea chloroplasts

doi: 10.3389/fpls.2014.00239

Figure Lengend Snippet: The extreme N-terminus of FSD1 is not sufficient for guiding a reporter into chloroplasts . Arabidopsis mesophyll protoplasts were transiently transformed with C-terminal GFP fusions to either full-length FSD1 or the indicated number of N-terminal amino acids. Maximum intensity signals from confocal images are shown for GFP fluorescence (GFP), chlorophyll autofluorescence (chl) and an overlay of both (merge). The used constructs are depicted on the left. AA , amino acids; bar, 5 μm.

Article Snippet: Outer envelope membranes were prepared from pea chloroplasts according to Cline et al. ( ) and incubated with a synthetic peptide representing the N-terminal region of FSD1 (amino acids 1–25) carrying a C-terminal biotin-moiety (JPT Peptide Technologies GmbH, Berlin, Germany) in the presence of 0.1 mM ATP at 4°C for 5 min. After recovery of the membranes by centrifugation they were treated with 5 mM of N-(α-Maleimidoacetoxy) succinimide ester (AMAS, Thermo Fisher Scientific, Schwerte, Germany) for 30 min on ice to initiate cross-linking.

Techniques: Transformation Assay, Fluorescence, Construct

Journal: Frontiers in Plant Science

Article Title: A new member of the psToc159 family contributes to distinct protein targeting pathways in pea chloroplasts

doi: 10.3389/fpls.2014.00239

Figure Lengend Snippet: The extreme C-terminus of FSD1 is not necessary for import . In vitro import assays into pea chloroplasts are shown. Lane 1 represents 10% of translation product, Thl (+) indicates thermolysin digestion after the import reaction (lane 3). Asterisks indicate lower bands probably arising from post-translational modifications such as processing of the first methionine. Representative results from n = 3 independent experiments are depicted.

Article Snippet: Outer envelope membranes were prepared from pea chloroplasts according to Cline et al. ( ) and incubated with a synthetic peptide representing the N-terminal region of FSD1 (amino acids 1–25) carrying a C-terminal biotin-moiety (JPT Peptide Technologies GmbH, Berlin, Germany) in the presence of 0.1 mM ATP at 4°C for 5 min. After recovery of the membranes by centrifugation they were treated with 5 mM of N-(α-Maleimidoacetoxy) succinimide ester (AMAS, Thermo Fisher Scientific, Schwerte, Germany) for 30 min on ice to initiate cross-linking.

Techniques: In Vitro

Journal: Frontiers in Plant Science

Article Title: A new member of the psToc159 family contributes to distinct protein targeting pathways in pea chloroplasts

doi: 10.3389/fpls.2014.00239

Figure Lengend Snippet: psToc120A domain has specific recognition motifs in FSD1 . PepSpot assays were designed and spotted onto filter paper where each peptide represents consecutively 15 AA with an overlap of 12 AA. In total, 67 peptides were spotted; the last 13 spots of the membrane are devoid of peptide. (A) Heterologously expressed psToc120A was incubated with the filters and detected by immunoblotting with a specific antibody against psToc120A. (B) Prominently bound peptides are marked in gray in the FSD1 sequence and the deducted binding regions are numbered form one to six in gray boxes.

Article Snippet: Outer envelope membranes were prepared from pea chloroplasts according to Cline et al. ( ) and incubated with a synthetic peptide representing the N-terminal region of FSD1 (amino acids 1–25) carrying a C-terminal biotin-moiety (JPT Peptide Technologies GmbH, Berlin, Germany) in the presence of 0.1 mM ATP at 4°C for 5 min. After recovery of the membranes by centrifugation they were treated with 5 mM of N-(α-Maleimidoacetoxy) succinimide ester (AMAS, Thermo Fisher Scientific, Schwerte, Germany) for 30 min on ice to initiate cross-linking.

Techniques: Membrane, Incubation, Western Blot, Sequencing, Binding Assay

Journal: Frontiers in Plant Science

Article Title: A new member of the psToc159 family contributes to distinct protein targeting pathways in pea chloroplasts

doi: 10.3389/fpls.2014.00239

Figure Lengend Snippet: The fifth recognition motif in the C-proximal end of FSD1 import is essential for binding and import. (A) Schematic representation of the constructs used for import in (B). (B) In vitro import assays of C-terminal truncations are depicted. Lane 1 shows 10% of translation product. Thl (+) indicates thermolysin digestion after the import reaction (lanes 3, 6, 9). Numbers on the left indicate size markers in kDa. Representative results from n = 3 independent experiments are depicted.

Article Snippet: Outer envelope membranes were prepared from pea chloroplasts according to Cline et al. ( ) and incubated with a synthetic peptide representing the N-terminal region of FSD1 (amino acids 1–25) carrying a C-terminal biotin-moiety (JPT Peptide Technologies GmbH, Berlin, Germany) in the presence of 0.1 mM ATP at 4°C for 5 min. After recovery of the membranes by centrifugation they were treated with 5 mM of N-(α-Maleimidoacetoxy) succinimide ester (AMAS, Thermo Fisher Scientific, Schwerte, Germany) for 30 min on ice to initiate cross-linking.

Techniques: Binding Assay, Construct, In Vitro

Journal: Frontiers in Plant Science

Article Title: A new member of the psToc159 family contributes to distinct protein targeting pathways in pea chloroplasts

doi: 10.3389/fpls.2014.00239

Figure Lengend Snippet: Hypothetical model for dynamic TOC complexes . The general import pathway comprises Toc159, Toc34, and Toc75 as core components. The hypothetical translocon responsible for FSD1 import consists of Toc120, most likely Toc75 and unknown component(s). Green color indicates the pathway taken by canonical substrates, whereas orange signifies an alternative translocon. A mix of both colors indicates participation in both translocation machineries. Thus, Toc75 as the common channel can form a complex with both Toc120 and Toc159, but not necessarily at the same time.

Article Snippet: Outer envelope membranes were prepared from pea chloroplasts according to Cline et al. ( ) and incubated with a synthetic peptide representing the N-terminal region of FSD1 (amino acids 1–25) carrying a C-terminal biotin-moiety (JPT Peptide Technologies GmbH, Berlin, Germany) in the presence of 0.1 mM ATP at 4°C for 5 min. After recovery of the membranes by centrifugation they were treated with 5 mM of N-(α-Maleimidoacetoxy) succinimide ester (AMAS, Thermo Fisher Scientific, Schwerte, Germany) for 30 min on ice to initiate cross-linking.

Techniques: Translocation Assay

Journal: Progress in Earth and Planetary Science

Article Title: Cold-based glaciation of Pavonis Mons, Mars: evidence for moraine deposition during glacial advance

doi: 10.1186/s40645-020-0323-9

Figure Lengend Snippet: Topography of the Arsia and Pavonis FSDs. a A true color image mosaic from Viking data of the western hemisphere of Mars. b Detailed elevation (colored regions) of the FSDs (outlined with black/white dotted line) indicate rougher topography within the FSDs and presence of volcanic rifts at Arsia. White line with labeled distances gives the location of the flowline used in numerical model. c HRSC image of the outer margin of the Arsia FSD where the intersection of moraine-like ridges (arrows) indicates that glacial activity was not capable of eroding previous ridges during subsequent glacial advance

Article Snippet: The fan-shaped deposits (FSDs) on the Tharsis volcanoes (Arsia, Pavonis, and Ascraeus) (Fig. a) were first described in detail using images from the Mariner 9 and Viking missions (Zimbelman and Edgett ).

Techniques: Western Blot, Labeling, Activity Assay

Journal: Progress in Earth and Planetary Science

Article Title: Cold-based glaciation of Pavonis Mons, Mars: evidence for moraine deposition during glacial advance

doi: 10.1186/s40645-020-0323-9

Figure Lengend Snippet: Topography and morphology of the distal portion of the Arsia ( a ) and Pavonis ( b ) FSDs. CTX imagery and transparent stereo topography (colored regions) shows ridge sequences of parallel ridges together with smooth (labeled with “S”) and knobby (labeled with “K”) units. The smooth unit (interpreted as remnant debris-covered ice by Shean et al. ) superposes ridges in the Pavonis FSD and indicates that the flow of ice responsible for forming the smooth unit was not erosive. Ridge spacing and cross-sectional area measurements using this data are shown in Figs. and

Article Snippet: The fan-shaped deposits (FSDs) on the Tharsis volcanoes (Arsia, Pavonis, and Ascraeus) (Fig. a) were first described in detail using images from the Mariner 9 and Viking missions (Zimbelman and Edgett ).

Techniques: Labeling