Привет друзья. Наше знакомство продолжается с новым фотоцветущим растением от Smail_Seeds сорт ORIGINAL CHEMZKITTLEZ F1 reg. Сегодня растению 83 дня. Перевёл на 12/12 1.10.2023 Растение очень хорошо развивается, ни каких сбоев в генетике не наблюдается😀 Сорт выводим сами. Смотри мой профиль, у нас всегда есть что то интересное. Не забудь поставить лайк❤️, если понравилась как прошла неделя И читайте наш TELEGRAM: https://t.me/smail_seeds #Smail_Seeds 😀

Week 9 of Flower - Beautiful colours and a crazy smell

Day 14, Two of the Orange Sherbets are a little behind & the one I’m trying to pull back from nutrient burn.. So far the White Widow Autos by Seedsman have been doing the best! Day 17 two of the Orange sherbet are a little behind the rest of the plants but overall I would say everything is going good! Seems like the orange sherbet that had the nutrient burn is starting to bounce back! Day 19 They are all really starting to take off! Probably gonna do some LST tonight or tomorrow!

This week the weather is better. The buds are getting fat and she is developing well. Terpes are amazing, sweet fruits and fresh mint.

Week 10 day 64 The temperatures are still not so high as they were before but it is still 25 degrees celsius outside. ( 77 Fh). So temperatures inside are better manageable. I started again with the feed with the auto Zkittelz. Video Music: Activation URL: https://icons8.com/music/

Easy to train and flowers fast

Not even sure if they’re actually in week 10 haven’t really been taking too many pictures. Really loving the gorilla cookies and how big they are vs the apricot auto in the closer left corner. All other 3 are gorilla cookies autos. Just started feeding just distilled water for now and flush them to get for hatbest

I figured I would not bore everyone with veg photos. EMERALD TRIANGLE SEEDS —-Sherbet Dip—- Sherbert x Amnesia Growing in a 2 gallon pot In Detroit Nutrient Company LIVING SOIL! Was Fed WATER ONLY in veg. She was flipped to flower 5 days ago. She was lolipopped Looking really nice! Going to start the bloom nutrients this next week! ✌️🏻💚🌿💨

Day 77 Mon PH 5.7 EC 0.9 DLI 12h PPFD Water 20 Day 78 Tue Add bloom B and ph up PH 5.0 - 5.9 EC 0.9 - 1.2 DLI 12h PPFD Water 22 Day 79 Wed Add Ph Up PH 4.4 - 6.0 EC 1.2 - 1.3 DLI 12h PPFD Water 20 Day 80 Thu Refresh water and nuts PH 6.0 EC 0.6 DLI 12h PPFD Water 26c Day 81 Fri Add Ph Down PH 7.0 - 5.9 EC 0.6 - 0.7 DLI 12h PPFD Water 24c Day 82 Sat Add Ph Up PH 5.5 - 5.9 EC 0.7 DLI 12h PPFD Water 23c Day 83 Sun PH 5.9 EC 0.7 DLI 12h PPFD Water 23c

Day 56 -looking good for the most part. however i ahve onethat just turned completly yellow. i gave it some calmag, but IDK...

ANTHOCYANIN production is primarily controlled by the Cryptochrome (CR1) Photoreceptor ( !! UV and Blue Spectrums are primary drivers in the production of the pigment that replaces chlorophyll, isn't that awesome! 1. Diverse photoreceptors in plants Many civilizations, including the sun god of ancient Egypt, thought that the blessings of sunlight were the source of life. In fact, the survival of all life, including humans, is supported by the photosynthesis of plants that capture solar energy. Plants that perform photosynthesis have no means of transportation except for some algae. Therefore, it is necessary to monitor various changes in the external environment and respond appropriately to the place to survive. Among various environmental information, light is especially important information for plants that perform photosynthesis. In the process of evolution, plants acquired phytochrome, which mainly receives light in the red light region, and multiple blue light receptors, including his hytropin and phototropin, in order to sense the light environment. .. In addition to these, an ultraviolet light receptor named UVR8 was recently discovered. The latest image of the molecular structure and function of these various plant photoreceptors (Fig. 1), focusing on phytochrome and phototropin. Figure 1 Ultraviolet-visible absorption spectra of phytochrome, cryptochrome, phototropin, and UVR8. The dashed line represents each bioactive absorption spectrum. 2. Phytochrome; red-far red photoreversible molecular switch What is phytochrome? Phytochrome is a photochromic photoreceptor, and has two absorption types, a red light absorption type Pr (absorption maximum wavelength of about 665 nm) and a far-red light absorption type Pfr (730 nm). Reversible light conversion between the two by red light and far-red light, respectively(Fig. 1A, solid line and broken line). In general, Pfr is the active form that causes a physiological response. With some exceptions, phytochrome can be said to function as a photoreversible molecular switch. The background of the discovery is as follows. There are some types of plants that require light for germination (light seed germination). From that study, it was found that germination was induced by red light, the effect was inhibited by subsequent far-red light irradiation, and this could be repeated, and the existence of photoreceptors that reversibly photoconvert was predicted. In 1959, its existence was confirmed by the absorption spectrum measurement of the yellow sprout tissue, and it was named phytochrome. Why does the plant have a sensor to distinguish between such red light and far-red light? There is no big difference between the red and far-red light regions in the open-field spectrum of sunlight, but the proportion of red light is greatly reduced due to the absorption of chloroplasts in the shade of plants. Similar changes in light quality occur in the evening sunlight. Plants perceive this difference in light quality as the ratio of Pr and Pfr, recognize the light environment, and respond to it. Subsequent studies have revealed that it is responsible for various photomorphogenic reactions such as photoperiodic flowering induction, shade repellent, and deyellowing (greening). Furthermore, with the introduction of the model plant Arabidopsis thaliana (At) and the development of molecular biological analysis methods, research has progressed dramatically, and his five types of phytochromes (phyA-E) are present in Arabidopsis thaliana. all right. With the progress of the genome project, Fi’s tochrome-like photoreceptors were found in cyanobacteria, a photosynthetic prokaryotes other than plants. Furthermore, in non-photosynthetic bacteria, a homologue molecule called bacteriophytochrome photoreceptor (BphP) was found in Pseudomonas aeruginosa (Pa) and radiation-resistant bacteria (Deinococcus radiodurans, Dr). Domain structure of phytochrome molecule Phytochrome molecule can be roughly divided into N-terminal side and C-terminal side region. PAS (Per / Arndt / Sim: blue), GAF (cGMP phosphodiesterase / adenylyl cyclase / FhlA: green), PHY (phyto-chrome: purple) 3 in the N-terminal region of plant phytochrome (Fig. 2A) There are two domains and an N-terminal extension region (NTE: dark blue), and phytochromobilin (PΦB), which is one of the ring-opening tetrapyrroles, is thioether-bonded to the system stored in GAF as a chromophore. ing. PAS is a domain involved in the interaction between signal transduction-related proteins, and PHY is a phytochrome-specific domain. There are two PASs and her histidine kinase-related (HKR) domain (red) in the C-terminal region, but the histidine essential for kinase activity is not conserved. 3. Phototropin; photosynthetic efficiency optimized blue light receptor What is phototropin? Charles Darwin, who is famous for his theory of evolution, wrote in his book “The power of move-ment in plants” published in 1882 that plants bend toward blue light. Approximately 100 years later, the protein nph1 (nonphoto-tropic hypocotyl 1) encoded by one of the causative genes of Arabidopsis mutants causing phototropic abnormalities was identified as a blue photoreceptor. Later, another isotype npl1 was found and renamed phototropin 1 (phot1) and 2 (phot2), respectively. In addition to phototropism, phototropin is damaged by chloroplast photolocalization (chloroplasts move through the epidermal cells of the leaves and gather on the cell surface under appropriate light intensity for photosynthesis. As a photoreceptor for reactions such as escaping to the side of cells under dangerous strong light) and stomata (reactions that open stomata to optimize the uptake of carbon dioxide, which is the rate-determining process of photosynthetic reactions). It became clear that it worked. In this way, phototropin can be said to be a blue light receptor responsible for optimizing photosynthetic efficiency. Domain structure and LOV photoreaction of phototropin molecule Phototropin molecule has two photoreceptive domains (LOV1 and LOV2) called LOV (Light-Oxygen-Voltage sensing) on the N-terminal side, and serine / on the C-terminal side. It is a protein kinase that forms threonine kinase (STK) (Fig. 4Aa) and whose activity is regulated by light. LOV is one molecule as a chromophore, he binds FMN (flavin mononucleotide) non-covalently. The LOV forms an α/βfold, and the FMN is located on a β-sheet consisting of five antiparallel β-strands (Fig. 4B). The FMN in the ground state LOV shows the absorption spectrum of a typical oxidized flavin protein with a triplet oscillation structure and an absorption maximum wavelength of 450 nm, and is called D450 (Fig. 1C and Fig. 4E). After being excited to the singlet excited state by blue light, the FMN shifts to the triplet excited state (L660t *) due to intersystem crossing, and then the C4 (Fig. 4C) of the isoaroxazine ring of the FMN is conserved in the vicinity. It forms a transient accretionary prism with the tain (red part in Fig. 4B Eα) (S390I). When this cysteine is replaced with alanine (C / A substitution), the addition reaction does not occur. The effect of adduct formation propagates to the protein moiety, causing kinase activation (S390II). After that, the formed cysteine-flavin adduct spontaneously dissociates and returns to the original D450 (Fig. 4E, dark regression reaction). Phototropin kinase activity control mechanism by LOV2 Why does phototropin have two LOVs? Atphot1 was found as a protein that is rapidly autophosphorylated when irradiated with blue light. The effect of the above C / A substitution on this self-phosphorylation reaction and phototropism was investigated, and LOV2 is the main photomolecular switch in both self-phosphorylation and phototropism. It turns out that it functions as. After that, from experiments using artificial substrates, STK has a constitutive activity, LOV2 functions as an inhibitory domain of this activity, and the inhibition is eliminated by photoreaction, while LOV1 is kinase light. It was shown to modify the photosensitivity of the activation reaction. In addition to this, LOV1 was found to act as a dimerization site from the crystal structure and his SAXS. What kind of molecular mechanism does LOV2 use to photoregulate kinase activity? The following two modules play important roles in this intramolecular signal transduction. Figure 4 (A) Domain structure of LOV photoreceptors. a: Phototropin b: Neochrome c: FKF1 family protein d: Aureochrome (B) Crystal structure of auto barley phot1 LOV2. (C) Structure of FMN isoaroxazine ring. (D) Schematic diagram of the functional domain and module of Arabidopsis thaliana phot1. L, A’α, and Jα represent linker, A’α helix, and Jα helix, respectively. (E) LOV photoreaction. (F) Molecular structure model (mesh) of the LOV2-STK sample (black line) containing A’α of phot2 obtained based on SAXS under dark (top) and under bright (bottom). The yellow, red, and green space-filled models represent the crystal structures of LOV2-Jα, protein kinase A N-lobe, and C-robe, respectively, and black represents FMN. See the text for details. 1) Jα. LOV2 C of oat phot1-to α immediately after the terminus Rix (Jα) is present (Fig. 4D), which interacts with the β-sheet (Fig. 4B) that forms the FMN-bound scaffold of LOV2 in the dark, but unfolds and dissociates from the β-sheet with photoreaction. It was shown by NMR that it does. According to the crystal structure of LOV2-Jα, this Jα is located on the back surface of the β sheet and mainly has a hydrophobic interaction. The formation of S390II causes twisting of the isoaroxazine ring and protonation of N5 (Fig. 4C). As a result, the glutamine side chain present on his Iβ strand (Fig. 4B) in the β-sheet rotates to form a hydrogen bond with this protonated N5. Jα interacts with this his Iβ strand, and these changes are thought to cause the unfold-ing of Jα and dissociation from the β-sheet described above. Experiments such as amino acid substitution of Iβ strands revealed that kinases exhibit constitutive activity when this interaction is eliminated, and that Jα plays an important role in photoactivation of kinases. 2) A’α / Aβ gap. Recently, several results have been reported showing the involvement of amino acids near the A’α helix (Fig. 4D) located upstream of the N-terminal of LOV2 in kinase photoactivation. Therefore, he investigated the role of this A’α and its neighboring amino acids in kinase photoactivation, photoreaction, and Jα structural change for Atphot1. The LOV2-STK polypeptide (Fig. 4D, underlined in black) was used as a photocontrollable kinase for kinase activity analysis. As a result, it was found that the photoactivation of the kinase was abolished when amino acid substitution was introduced into the A’α / Aβ gap between A’α and Aβ of the LOV2 core. Interestingly, he had no effect on the structural changes in Jα examined on the peptide map due to the photoreaction of LOV2 or trypsin degradation. Therefore, the A’α / Aβ gap is considered to play an important role in intramolecular signal transduction after Jα. Structural changes detected by SAXS Structural changes of Jα have been detected by various biophysical methods other than NMR, but structural information on samples including up to STK is reported only by his results to his SAXS. Not. The SAXS measurement of the Atphot2 LOV2-STK polypeptide showed that the radius of inertia increased from 32.4 Å to 34.8 Å, and the molecular model (Fig. 4F) obtained by the ab initio modeling software GASBOR is that of LOV2 and STK. It was shown that the N lobes and C lobes lined up in tandem, and the relative position of LOV2 with respect to STK shifted by about 13 Å under light irradiation. The difference in the molecular model between the two is considered to reflect the structural changes that occur in the Jα and A’α / Aβ gaps mentioned above. Two phototropins with different photosensitivity In the phototropic reaction of Arabidopsis Arabidopsis, Arabidopsis responds to a very wide range of light intensities from 10–4 to 102 μmol photon / sec / m2. At that time, phot1 functions as an optical sensor in a wide range from low light to strong light, while phot2 reacts with light stronger than 1 μmol photon / sec / m2. What is the origin of these differences? As is well known, animal photoreceptors have a high photosensitivity due to the abundance of rhodopsin and the presence of biochemical amplification mechanisms. The exact abundance of phot1 and phot2 in vivo is unknown, but interesting results have been obtained in terms of amplification. The light intensity dependence of the photoactivation of the LOV2-STK polypeptide used in the above kinase analysis was investigated. It was found that phot1 was about 10 times more photosensitive than phot2. On the other hand, when the photochemical reactions of both were examined, it was found that the rate of the dark return reaction of phot1 was about 10 times slower than that of phot2. This result indicates that the longer the lifetime of S390II, which is in the kinase-activated state, the higher the photosensitivity of kinase activation. This correlation was further confirmed by extending the lifespan of her S390II with amino acid substitutions. This alone cannot explain the widespread differences in photosensitivity between phot1 and phot2, but it may explain some of them. Furthermore, it is necessary to investigate in detail protein modifications such as phosphorylation and the effects of phot interacting factors on photosensitivity. Other LOV photoreceptors Among fern plants and green algae, phytochrome ɾphotosensory module (PSM) on the N-terminal side and chimera photoreceptor with full-length phototropin on the C-terminal side, neochrome (Fig. There are types with 4Ab). It has been reported that some neochromes play a role in chloroplast photolocalization as a red light receiver. It is considered that fern plants have such a chimera photoreceptor in order to survive in a habitat such as undergrowth in a jungle where only red light reaches. In addition to this, plants have only one LOV domain, and three proteins involved in the degradation of photomorphogenesis-related proteins, FKF1 (Flavin-binding, Kelch repeat, F-box 1, ZTL (ZEITLUPE)), LKP2 ( There are LOV Kelch Protein2) (Fig. 4Ac) and aureochrome (Fig. 4Ad), which has a bZip domain on the N-terminal side of LOV and functions as a gene transcription factor. 4. Cryptochrome and UVR8 Cryptochrome is one of the blue photoreceptors and forms a superfamily with the DNA photoreceptor photolyase. It has FAD (flavin adenine dinucle-otide) as a chromophore and tetrahydrofolic acid, which is a condensing pigment. The ground state of FAD is considered to be the oxidized type, and the radical type (broken line in Fig. 1B) generated by blue light irradiation is considered to be the signaling state. The radical type also absorbs in the green to orange light region, and may widen the wavelength region of the plant morphogenesis reaction spectrum. Cryptochrome uses blue light to control physiological functions similar to phytochrome. It was identified as a photoreceptor from one of the causative genes of UVR8 Arabidopsis thaliana, and the chromophore is absorbed in the UVB region by a Trp triad consisting of three tryptophans (Fig. 1D). It is involved in the biosynthesis of flavonoids and anthocyanins that function as UV scavengers in plants. Conclusion It is thought that plants have acquired various photoreceptors necessary for their survival during a long evolutionary process. The photoreceptors that cover the existing far-red light to UVB mentioned here are considered to be some of them. More and more diverse photoreceptor genes are conserved in cyanobacteria and marine plankton. By examining these, it is thought that the understanding of plant photoreceptors will be further deepened.

2-1 Got her first water in new home. Was not watered in during x plant. Let her dry what she had first. 7ml EM1 will get a bigger dose soon. Just to kick things off. Around 1/2 tsp recharge, 1ml drops of balance. 1.5 ml Silica. Ph 6.0 500 ml. 2-3 Wish I would have watered 250-300. 500 was a bit much, should be fine. Looks very happy and perky. 2-4 Looks like she may have the fungus. Removed first leaves. 2-5 Peroxide spray at lights out. Slight possibility on 2nd set of leaves. 2-6 Removed 3rd set up leaves. Oh my goodness not again! Foliar spray, Canncontrol 300ml water .8 ml CannC. As a precaution. Enlisted Valiotoro, light may have burnts when lights came on from foliar. I dont remember checking. Focused more on if spread. 😂 Hope this helps. 🤞 Sad that the leaf removal will slow her down. .

Oggi, lunedì 22/01 ho cambiato una 40 ina di litri di soluzione nuova e fresca...ho notato che verso la fine, l'acqua/soluzione era più "limpida" rispetto alla prima ventina di litri ... credo che la pietra porosa con aggiunta di ossigenatore sia stata utile nel secchio "Sistema" per evitare eventuali depositi sul fondo Il problema maggiore è la temperatura stessa ossigenata... è impossibile tenerla a 19/20° senza l'uso di un raffreddatore(Chiller)...costa un botto! Ora è a 21.3 ma sicuramente salirà....di solito è intorno ai 22° ...La luce led dimmerabile è all'80%... È vero che ci saranno le foglie a fare ombra al vaso....ma non so se al 100% ,che metterò ad inizio fioritura e l'abbassero in altezza a 40 cm dalla cima,cosa accadrà alla temperatura,in generale Per ora andiamo avanti e proviamo a risolvere una cosa la volta 😉 Oggi topping o FiMing, vediamo cosa riesce😂 Crescono ma... credo che abbiano preso il Mosaico del tabacco..una malattia che deforma le foglie,si piegano le punte in su e in giù, alcune foglie appunto presentano una specie di mosaico con macchie giallognolo Sembra bene...oggi 2 febbraio defogliazione e da lunedì si passa alle 12 ore..... credo che farò così...o farò poi fatica a gestire le altezze e l'area...ho notato che le foglie e il tronco sono molto più grossi rispetto la terra con lo stesso periodo di 3 settimane piene...

Idhdb

Très satisfait de cette variété. Ma favorite a se moment. Satisfait des 56 grammes que j'ai pu y récolté. Durant la troisième semaines de floraison j'ai eu une petite crainte en trouvent 7 banane que j'ai enlever a la pince a cils. 2 était éclos. Finalement je suis contant de cette situation car j'ai pus recueillir 8 graines sur quelques petit bourgeon. En gros, très bonne souche. 👍👌

the cutting time has arrived!! It's time to taste it, it smells really good, but not at all like the fresh plant, I'm a little disappointed.. after drying and curing, the variety smells like bananas, very ripe yellow fruit, with an earthy and sweet background!! it's very round in the mouth, very sweet and resinous, but there's some rubbish in the taste, on the exhilaration it's a bit acrid.. I missed the drying, the heads are compact but cottony... I will succeed better next time!! see you

Привет друзья. Моей растихе сегодня 71 дней. Был в отъезеде, не поливал. В связи этим растение не много подсохло. Как придёт в чувства. переведу на цвет. Начал применять LST технику на 19 дне и продалжаю применять её через день, а 18 августа добавил ДЕФОЛИЗАЦИЮ С 20.08 ДЕФОЛИЗАЦИЮ делаю каждые 3,4 дня С 20.08 LST технику делаю каждые 4.6 дней На сегодняшний день влажность 54% 26 дней назад заметил высокий Ph 7.9 С 48 дня Ph не ниже 5.8 На сегодняшний день Ph 6.0 Начал кормить с 60 дня Canna Terra Vega PPM 550 Погладитель влажности, выполняет свои функции. Посмотрю на динамику. Всем мира и добра! https://t.me/smail_seeds #Smail_Seeds