36 research outputs found
Evaluation of tuberose genotype IIHR 17-23SP-08 (IC0642158) for flower yield, quality and response to biotic stress
Tuberose (Agave amica, family Asparagaceae) is an important commercial flower crop valued for its spectacular fragrant flowers. An experiment was conducted to evaluate the single petalled tuberose genotypes for growth, flowering, flower yield, concrete yield and response to biotic stress for two consecutive years from 2020 to 2022. Tuberose genotype IIHR 17-23SP-08 was found to be superior with highest plant height (55.53 cm), early flowering (94.93 days), highest number of spikes/plant (8.47), longest spikes (114.61cm) and rachis (32.11cm) and maximum number of florets/spike (54.87). The matured bud weight of IIHR 17-23SP-08 was 1.29 g, which is preferable in the medium segment range with higher number of flower buds (725 buds per kg). It is a high yielder producing the highest number of spikes/m2 (76.20) and loose flower yield 18.88 t/ha/year among the genotypes evaluated. The genotype IIHR 17-23SP-08 was also found to be a good multiplier with the maximum bulb production of 8.94 bulbs per clump. It was found to be resistant to root knot nematode (Meloidogyne incognita) and tolerant to leaf burn disease (Alternaria polianthi) under field conditions. It was found suitable as loose flower for garland preparation with the shelf life of 2 days under ambient conditions and for concrete extraction with the concrete yield of 0.095%. It produces white buds (RHS colour: NNI55D, white group, Fan 4) with green tinge on the tip. Thus, the genotype IIHR 17 23SP 08 was found promising and novel among the single types with better flower and bulb yield parameters
Hydrogen Transfer Reduction of Aldehydes with Alkali-Metal Carbonates and Ir NHC Complexes
Way toward “Dietary Pesticides”: Molecular Investigation of Insecticidal Action of Caffeic Acid against <i>Helicoverpa armigera</i>
Bioprospecting
of natural molecules is essential to overcome serious
environmental issues and pesticide resistance in insects. Here we
are reporting insights into insecticidal activity of a plant natural
phenol. In silico and in vitro screening of multiple molecules supported
by in vivo validations suggested that caffeic acid (CA) is a potent
inhibitor of <i>Helicoverpa armigera</i> gut proteases.
Protease activity and gene expression were altered in CA-fed larvae.
The structure–activity relationship of CA highlighted that
all the functional groups are crucial for inhibition of protease activity.
Biophysical studies and molecular dynamic simulations revealed that
sequential binding of multiple CA molecules induces conformational
changes in the protease(s) and thus lead to a significant decline
in their activity. CA treatment significantly inhibits the insect’s
detoxification enzymes, thus intensifying the insecticidal effect.
Our findings suggest that CA can be implicated as a potent insecticidal
molecule and explored for the development of effective dietary pesticides
Structural and optical properties of polycrystalline NiO thin films prepared by using the oxidation of the metallic Ni
Here, we report on the structural and the optical properties of polycrystalline NiO thin films prepared by using the thermal oxidation of metallic Ni. After the deposition of the Ni films, they were placed in a thermal oxidation furnace at different temperatures (400, 500, 600, 700, and 1000 ??C), resulting in mean crystallite sizes between 6 nm and 40 nm. From the optical absorption spectra, we determined the energy gaps of these films. Interestingly, the energy gaps were in the range of 3.13 ??? 3.29 eV, which were smaller than those of the bulk.ope
Regio- and Chemoselective Catalytic Transfer Hydrogenation of Aromatic Nitro and Carbonyl as Well as Reductive Cleavage of Azo Compounds over Novel Mesoporous NiMCM-41 Molecular Sieves
Atomistic molecular dynamics simulations on the interaction of TEMPO-oxidized cellulose nanofibrils in water
An alternative flexible conformation of the E. coli HUbeta(2) protein: structural, dynamics, and functional aspects.
The histone-like HU protein is the major nucleoid-associated protein involved in the dynamics and structure of the bacterial chromosome. Under physiological conditions, the three possible dimeric forms of the E. coli HU protein (EcHUalpha(2), EcHUbeta(2), and EcHUalphabeta) are in thermal equilibrium between two dimeric conformations (N(2) I(2)) varying in their secondary structure content. High-temperature molecular dynamics simulations combined with NMR experiments provide information about structural and dynamics features at the atomic level for the N(2) to I(2) thermal transition of the EcHUbeta(2) homodimer. On the basis of these data, a realistic 3D model is proposed for the major I(2) conformation of EcHUbeta(2). This model is in agreement with previous experimental data