Imagine packing all the people in the world into the Great Salt Lake in Utah — all of us jammed shoulder to shoulder, yet also charging past one another at insanely high speeds. That gives you some idea of how densely crowded the 5 billion proteins in a typical cell are, said Anthony Hyman, a British cell biologist and a director of the Max Planck Institute of Molecular Cell Biology and Genetics in Dresden.
Somehow in that bustling cytoplasm, enzymes need to find their substrates, and signaling molecules need to find their receptors, so the cell can carry out the work of growing, dividing and surviving. If cells were sloshing bags of evenly mixed cytoplasm, that would be difficult to achieve. But they are not. Membrane-bounded organelles help to organize some of the contents, usefully compartmentalizing sets of materials and providing surfaces that enable important processes, such as the production of ATP, the biochemical fuel of cells. But, as scientists are still only beginning to appreciate, they are only one source of order.
Recent experiments reveal that some proteins spontaneously gather into transient assemblies called condensates, in response to molecular forces that precisely balance transitions between the formation and dissolution of droplets inside the cell. Condensates, sometimes referred to as membraneless organelles, can sequester specific proteins from the rest of the cytoplasm, preventing unwanted biochemical reactions and greatly increasing the efficiency of useful ones. These discoveries are changing our fundamental understanding of how cells work.
For instance, condensates may explain the speed of many cellular processes. “The key thing about a condensate — it’s not like a factory; it’s more like a flash mob. You turn on the radio, and everyone comes together, and then you turn it off and everyone disappears,” Hyman said.
As such, the mechanism is “exquisitely regulatable,” said Gary Karpen, a cell biologist at the University of California, Berkeley, and the Lawrence Berkeley National Laboratory. “You can form these things and dissolve them quite readily by just changing concentrations of molecules” or chemically modifying the proteins. This precision provides leverage for control over a host of other phenomena, including gene expression.
The first hint of this mechanism arrived in the summer of 2008, when Hyman and his then-postdoctoral fellow Cliff Brangwynne (now a Howard Hughes Medical Institute investigator at Princeton University) were teaching at the famed Marine Biological Laboratory physiology course and studying the embryonic development of C. elegans roundworms. When they and their students observed that aggregates of RNA in the fertilized worm egg formed droplets that could split away or fuse with each other, Hyman and Brangwynne hypothesized that these “P granules” formed through phase separation in the cytoplasm, just like oil droplets in a vinaigrette.
That proposal, published in 2009 in Science, didn’t get much attention at the time. But more papers on phase separation in cells trickled out around 2012, including a key experiment in Michael Rosen’s lab at the University of Texas Southwestern Medical Center in Dallas, which showed that cell signaling proteins can also exhibit this phase separation behavior. By 2015, the stream of papers had turned into a torrent, and since then there’s been a veritable flood of research on biomolecular condensates, these liquid-like cell compartments with both elastic and viscous properties.
Now cell biologists seem to find condensates everywhere they look: in the regulation of gene expression, the formation of mitotic spindles, the assembly of ribosomes, and many more cellular processes in the nucleus and cytoplasm. These condensates aren’t just novel but thought-provoking: The idea that their functions emerge from the collective behaviors of the molecules has become the central concept in condensate biology, and it contrasts sharply with the classic picture of pairs of biochemical agents and their targets fitting together like locks and keys. Researchers are still figuring out how to probe the functionality of these emergent properties; that will require the development of new techniques to measure and manipulate the viscosity and other properties of tiny droplets in a cell.
What Drives Droplet Formation
When biologists were first trying to explain what drives the phase separation phenomenon behind condensation in living cells, the structure of the proteins themselves offered a natural place to start. Well-folded proteins typically have a mix of hydrophilic and hydrophobic amino acids. The hydrophobic amino acids tend to bury themselves inside the protein folds, away from water molecules, while the hydrophilic amino acids get drawn to the surface. These hydrophobic and hydrophilic amino acids determine how the protein folds and holds its shape.
But some protein chains have relatively few hydrophobic amino acids, so they have no reason to fold. Instead, these intrinsically disordered proteins (IDPs) fluctuate in form and engage in many weak multivalent interactions. IDP interactions were thought for years to be the best explanation for the fluidlike droplet behavior.
Last year, however, Brangwynne published a couple of papers highlighting that IDPs are important, but that “the field has gone too far in emphasizing them.” Most proteins involved in condensates, he says, have a common architecture with some structured domains and some disordered regions. To seed condensates, the molecules must have many weak multivalent interactions with others, and there’s another way to achieve that: oligomerization.
Oligomerization occurs when proteins bind to each other and form larger complexes with repeating units, called oligomers. As the concentration of proteins increases, so does the phase separation and the oligomer formation. In a talk at the American Society for Cell Biology meeting in December, Brangwynne showed that as the concentration of oligomers increases, the strength of their interactions eventually overcomes the nucleation barrier, the energy required to create a surface separating the condensate from the rest of the cytoplasm. At that point, the proteins are containing themselves within a droplet.
In the past five years, researchers have taken big strides in understanding how this collective behavior of proteins arises from tiny physical and chemical forces. But they are still learning how (and whether) cells actually use this phenomenon to grow and divide.
Condensates and Gene Expression
Condensates seem to be involved in many aspects of cellular biology, but one area that has received particular attention is gene expression and the production of proteins.
Ribosomes are cells’ protein-making factories, and the number of them in a cell often limits its rate of growth. Work by Brangwynne and others suggests that fast-growing cells might get some help from the biggest condensate in the nucleus: the nucleolus. The nucleolus facilitates the rapid transcription of ribosomal RNAs by gathering up all of the required transcription machinery, including the specific enzyme (RNA polymerase I) that makes them.
A few years ago, Brangwynne and his then-postdoc Stephanie Weber, who is now an assistant professor at McGill University in Montreal, investigated how the size of the nucleolus (and therefore the speed of ribosomal RNA synthesis) was controlled in early C. elegans embryos. Because the mother worm contributes the same number of proteins to every embryo, small embryos have high concentrations of proteins and large embryos have low concentrations. And as the researchers reported in a 2015 Current Biology paper, the size of the nucleoli is concentration-dependent: Small cells have large nucleoli and large cells have small ones.
Brangwynne and Weber found that by artificially changing cell size, they could raise and lower the protein concentration and the size of the resulting nucleoli. In fact, if they lowered the concentration below a critical threshold, there was no phase separation and no nucleolus. The researchers derived a mathematical model based on the physics of condensate formation that could exactly predict the size of nucleoli in cells.
Now Weber is looking for condensates in bacteria, which have smaller cells and no membrane-bound compartments. “Maybe this is an even more important mechanism for compartmentalization, because they [bacteria] don’t have an alternative,” she suggested.
Last summer, Weber published a study showing that in cells of slow-growing E. coli bacteria, the RNA polymerase enzyme is uniformly distributed, but in fast-growing cells it clusters in droplets. The fast-growing cells may need to concentrate the polymerase around ribosomal genes to synthesize ribosomal RNA efficiently.
“It looks like it [phase separation] is in all domains of life, and a universal mechanism that has then been able to specialize into a whole bunch of different functions,” Weber said.
Although Weber and Brangwynne showed that active transcription occurs in one large condensate, the nucleolus, other condensates in the nucleus do the opposite. Large portions of the DNA in the nucleus are classified as heterochromatin because they are more compact and generally not expressed as proteins. In 2017, Karpen, Amy Strom (who is now a postdoc in Brangwynne’s lab) and their colleagues showed that a certain protein will undergo phase separation and form droplets on the heterochromatin in Drosophila embryos. These droplets can fuse with each other, possibly providing a mechanism for compacting heterochromatin inside the nucleus.
The results also suggested an exciting possible explanation for a long-standing mystery. Years ago, geneticists discovered that if they took an actively expressed gene and placed it right next to the heterochromatin, the gene would be silenced, as if the heterochromatin state was spreading. “This phenomenon of spreading was something that arose early on, and no one really understood it,” Karpen said.
Later, researchers discovered enzymes involved in epigenetic regulation called methyltransferases, and they hypothesized that the methyltransferases would simply proceed from one histone to the next down the DNA strand from the heterochromatin into the adjacent euchromatin, a kind of “enzymatic, processive mechanism,” Karpen said. This has been the dominant model to explain the spreading phenomenon for the last 20 years. But Karpen thinks that the condensates that sit on the heterochromatin, like wet beads on a string, could be products of a different mechanism that accounts for the spreading of the silent heterochromatin state. “These are fundamentally different ways to think about how the biology works,” he said. He’s now working to test the hypothesis.
The Formation of Filaments
Condensates also helped to solve a different cellular mystery — not inside the nucleus, but along the cell membrane. When a ligand binds to a receptor protein on a cell’s surface, it initiates a cascade of molecular changes and movements that convey a signal through the cytoplasm. But for that to happen, something first has to gather together all the dispersed players in the mechanism. Researchers now think phase separation might be a trick cells use to cluster the required signaling molecules at the membrane receptor, explains Lindsay Case, who trained in the Rosen lab as a postdoc and is starting her own lab at the Massachusetts Institute of Technology this month.
Case notes that protein modifications that are commonly used for transducing signals, such as the addition of phosphoryl groups, change the valency of a protein — that is, its capacity to interact with other molecules. The modifications therefore also affect proteins’ propensity to form condensates. “If you think about what a cell is doing, it is actually regulating this parameter of valency,” Case said.
Condensates may also play an important role in regulating and organizing the polymerization of small monomer subunits into long protein filaments. “Because you’re bringing molecules together for a longer period of time than you would outside the condensate, that favors polymerization,” Case said. In her postdoctoral research, she found that condensates enhance the polymerization of actin into filaments that help specialized kidney cells maintain their unusual shapes.
The polymerization of tubulin is key to the formation of the mitotic spindles that help cells divide. Hyman became interested in understanding the formation of mitotic spindles during his graduate studies in the Laboratory of Molecular Biology at the University of Cambridge in the 1980s. There, he studied how the single-celled C. elegans embryo forms a mitotic spindle before splitting into two cells. Now he’s exploring the role of condensates in this process.
In one in vitro experiment, Hyman and his team created droplets of the microtubule-binding tau protein and then added tubulin, which migrates into the tau droplets. When they added nucleotides to the drops to simulate polymerization, the tubulin monomers assembled into beautiful microtubules. Hyman and his colleagues have proposed that phase separation could be a general way for cells to initiate the polymerization of microtubules and the formation of the mitotic spindle.
The tau protein is also known for forming the protein aggregates that are the hallmarks of Alzheimer’s disease. In fact, many neurodegenerative conditions, such as amyotrophic lateral sclerosis (ALS) and Parkinson’s disease, involve the faulty formation of protein aggregates in cells.
To investigate how these aggregates might form, Hyman’s team focused on a protein called FUS that has mutant forms associated with ALS. The FUS protein is normally found in the nucleus, but in stressed cells, the protein leaves the nucleus and goes into the cytoplasm, where it forms into droplets. Hyman’s team found that when they made droplets of mutated FUS proteins in vitro, after only about eight hours the droplets solidified into what he calls “horrible aggregates.” The mutant proteins drove a liquid-to-solid phase transition far faster than normal form of FUS did.
Maybe the question isn’t why the aggregates form in disease, but why they don’t form in healthy cells. “One of the things I often ask in group meetings is: Why is the cell not scrambled eggs?” Hyman said in his talk at the cell biology meeting; the protein content of the cytoplasm is “so concentrated that it should just crash out of solution.”
A clue came when researchers in Hyman’s lab added the cellular fuel ATP to condensates of purified stress granule proteins and saw those condensates vanish. To investigate further, the researchers put egg whites in test tubes, added ATP to one tube and salt to the other, and then heated them. While the egg whites in the salt aggregated, the ones with ATP did not: The ATP was preventing protein aggregation at the concentrations found in living cells.
But how? It remained a puzzle until Hyman fortuitously met a chemist when presenting a seminar in Bangalore. The chemist noted that in industrial processes, additives called hydrotropes are used to increase the solubility of hydrophobic molecules. Returning to his lab, Hyman and his colleagues found that ATP worked exceptionally well as a hydrotrope.
Intriguingly, ATP is a very abundant metabolite in cells, with a typical concentration of 3-5 millimolar. Most enzymes that use ATP operate efficiently with concentrations three orders of magnitude lower. Why, then, is ATP so concentrated inside cells, if it isn’t needed to drive metabolic reactions?
One candidate explanation, Hyman suggests, is that ATP doesn’t act as a hydrotrope below 3-5 millimolar. “One possibility is that in the origin of life, ATP might have evolved as a biological hydrotrope to keep biomolecules soluble in high concentration and was later co-opted as energy,” he said.
It’s difficult to test that hypothesis experimentally, Hyman admits, because it is challenging to manipulate ATP’s hydrotropic properties without also affecting its energy function. But if the idea is correct, it might help to explain why protein aggregates commonly form in diseases associated with aging, because ATP production becomes less efficient with age.
Other Uses for Droplets
Protein aggregates are clearly bad in neurodegenerative diseases. But the transition from liquid to solid phases can be adaptive in other circumstances.
Take primordial oocytes, cells in the ovaries that can lie dormant for decades before maturing into an egg. Each of these cells has a Balbiani body, a large condensate of amyloid protein found in the oocytes of organisms ranging from spiders to humans. The Balbiani body is believed to protect mitochondria during the oocyte’s dormant phase by clustering a majority of the mitochondria together with long amyloid protein fibers. When the oocyte starts to mature into an egg, those amyloid fibers dissolve and the Balbiani body disappears, explains Elvan Böke, a cell and developmental biologist at the Center for Genomic Regulation in Barcelona. Böke is working to understand how these amyloid fibers assemble and dissolve, which could lead to new strategies for treating infertility or neurodegenerative diseases.
Protein aggregates can also solve problems that require very quick physiological responses, like stopping bleeding after injury. For example, Mucor circinelloides is a fungal species with interconnected, pressurized networks of rootlike hyphae through which nutrients flow. Researchers at the Temasek Life Sciences Laboratory led by the evolutionary cell biologist Greg Jedd recently discovered that when they injured the tip of a Mucor hypha, the protoplasm gushed out at first but almost instantaneously formed a gelatinous plug that stopped the bleeding.
Jedd suspected that this response was mediated by a long polymer, probably a protein with a repetitive structure. The researchers identified two candidate proteins and found that, without them, injured fungi catastrophically bled out into a puddle of protoplasm.
Jedd and his colleagues studied the structure of the two proteins, which they called gellin A and gellin B. The proteins had 10 repetitive domains, some of which had hydrophobic amino acids that could bind to cell membranes. The proteins also unfolded at forces similar to those they would experience when the protoplasm comes gushing out at the site of an injury. “There’s this massive acceleration in flow, and so we were thinking that maybe this is the trigger that is telling the gellin to change its state,” Jedd said. The plug, triggered by a physical cue that causes the gellin to transition from liquid to solid phase, is irreversibly solidified.
In contrast, in the fungal species Neurospora, the hyphae are divided into compartments, with pores that regulate the flow of water and nutrients. Jedd wanted to know how the pores were opened and closed. “What we discovered is some intrinsically disordered proteins that seem to be undergoing a condensation to aggregate at the pore, to provide a mechanism for closing it,” Jedd explained.
The Neurospora proteins that were candidates for this job, Jedd’s team learned, had repeated mixed-charge domains that could be found in some mammalian proteins, too. When the researchers synthesized proteins of varying compositions but with similar mixes of lengths and charge patterning and introduced them into mammalian cells, they found that the proteins could be incorporated into nuclear speckles, which are condensates in the mammalian cell nucleus that help to regulate gene expression, as they and colleagues led by Rohit Pappu of Washington University in St. Louis reported in a 2020 Molecular Cell paper.
The fungal and mammalian kingdoms seem to have arrived independently at a strategy of using disordered sequences in mechanisms based on condensation, Jedd said, “but they’re using it for entirely different reasons, in different compartments.”
Reconsidering Old Explanations
Phase separation has turned out to be ubiquitous, and researchers have generated lots of ideas about how this phenomenon could be involved in various cell functions. “There’s lots of exciting possibilities that [phase separation] raises, so that’s what I think drives … interest in the field,” Karpen said. But he also cautions that while it is relatively easy to show that a molecule undergoes phase separation in a test tube, demonstrating that phase separation has a function in the cell is much more challenging. “We still don’t know so much,” he said.
Brangwynne agreed. “If you’re really honest, it’s still pretty much at a hand-wavy stage, the whole field,” he said. “It’s very early days for understanding how this all works. The fact that it’s hand-wavy doesn’t mean that liquid phase separation isn’t the key driving force. In fact, I think it is. But how does it really work?”
The uncertainties do not discourage Hyman, either. “What phase separation is allowing everyone to do is go back and look at old problems which stalled out and think: Can we now think about this a different way?” he said. “All the structural biology that was done has just been brilliant — but many problems stalled out. They couldn’t actually explain things. And that’s what phase separation has allowed, is for everyone to think again about these problems.”
Russian Public Officials Have Until April to Sell Their Cryptocurrency Holdings
Several weeks after signing legislation that required Russian officials to disclose their crypto holdings, the world’s largest country by landmass has gone a step further by prohibiting them from owning any digital assets.
- The Ministry of Labor and Social Protection of the Russian Federation has sent a letter to civil servants regarding their cryptocurrency holdings, according to Forklog coverage. It reads that such officials have until April 1st, 2021, to get rid of their digital asset investments:
“Officials are obliged to dispose of digital financial assets issued in information systems organized in accordance with foreign law, as well as digital currency, regardless of the country of issue.”
- Apart from prohibiting civil servants from owning such assets, the letter also forbids officials from using them in any way, including as payment options.
- This decision comes shortly after President Vladimir Putin signed a decree dictating that country officials had to disclose information regarding their cryptocurrency investments. Those included the name of the assets that belong to them, their spouses, and minor children.
- Russia already has a somewhat controversial history with trying to regulate or even outlaw cryptocurrencies. Previous reports indicated that the nation considered hefty penalties and imprisonment for holding bitcoin above certain thresholds.
- The government rejected these propositions, and the new Prime Minister vowed to lead cryptocurrency usage in a “civilized direction.”
- Despite these setbacks, though, a recent report outlined that bitcoin is more attractive to Russian citizens than numerous other investment options, including gold.
Cardano, Cosmos, SushiSwap Price Analysis: 25 January
Cardano recovered from its drop to $0.285 and entered a phase of consolidation over the past few days. Cosmos formed a bullish triangle pattern but in the coming days was likely to see a drop to $7.15, should the $8 support not hold and SushiSwap had strong bullish momentum behind it as it targeted the $8.9 level of resistance.
Using the dip to $0.232 and the subsequent surge to $0.397 in mid-January, some Fibonacci retracement levels were plotted to highlight areas of support and resistance. ADA had appeared to form a range between $0.32 and $0.38, but the drop to $0.285 invalidated the range.
Over the past few days, ADA has traded sideways at the $0.34 level. Even though its recovery from the drop to $0.285 was quick, it has lost that upward momentum around the $0.35 price range.
The RSI highlighted this lack of momentum as it oscillated about the neutral 50 value. Losing the $0.35 level will see ADA revisit $0.32 as support. Trading volume was also low, showing a period of consolidation for ADA before its next move.
ATOM formed a descending triangle pattern, one that generally sees a breakout to the upside. Confirmation of direction would be a move with high trading volume, closing a session outside the pattern.
The $8 level of support could give way to short-term bearish pressure. This would see ATOM visit $7.15 and the market decide on the direction of the next move.
At the time of writing, the MACD showed neutral momentum.
SUSHI had strong bullish momentum behind it as it climbed past the region of supply at $7.5. After rising above this region on high trading volume, it could retest it as a region of demand in the coming days.
The OBV was also in an uptrend alongside the price, to show steady buying pressure behind the price hike. The next level of resistance for SUSHI is at $8.9.
Below $7.5, the $6 level is one of support for SUSHI.
Survival of the fittest: A look at how hash rate tokens compete with existing mining products and services
If you are a cryptocurrency and blockchain industry professional, the most commonly heard term would be computing power or hash rate, which is a quantitative measure of the computing speed of a mining machine. A new contender has entered the cryptocurrency mining scene – hash rate tokens.
What are they, and how do they impact the space as a whole? In this article, we explore what hash rate tokens are and compare them with other ways of mining, namely the use of cloud mining services, and running mining machines.
What exactly are hash rate tokens?
Hash rate tokens, also known as hash coins, tokenize the computing power of Bitcoin. A project hash rate token is equal to keeping its “corresponding Bitcoin mining power” and performance revenue is bound to the daily bitcoin mining profits. Unlike conventional cloud mining services, this model is equivalent to real-world mortgage assets.
Tokens are generated on the chain, providing a limited range of computing power assets with more liquidity. Mining can be carried out by holding hash rate coins to obtain mining income and by supporting flexible transactions, pledges, and other transactions that are convenient.
Token holders can also sell the hash rates they possess if they don’t want to generate profit from the hash rates.
There are currently two hash rate tokens on the market: Poolin Token (pBTC35A) and the Binance Hash coin, otherwise known as Bitcoin Standard Hash Rate Token, or BTCST. The hash rate token pBTC35A was launched by Poolin. On the other hand, BTCST was introduced by mining farms 360power and Ke Wo Ying Mining. The former has access to some mining services, while the latter is an over-the-counter transaction service provider for Binance Investments. At present, hash rate tokens are mostly Bitcoin-based, but support for other currencies – appear in the future.
Binance contributed greatly to the craze around hash rate tokens with BTCST. BTCST is a Bitcoin leveraged coin that is pegged to real-world computing power. While BTCST is currently a high-risk asset, the price of its currency has increased with the inclusion of its counterparts. Earlier, several media publications began to cover the leading players behind BTCST, namely Ke Wo Ying Mining and 360power, which were initially not major names in the industry. The frenzy is unlikely to end anytime soon. With the endorsement of Binance, hash rate tokens are poised to make a great impact.
Another value proposition of the hash rate token is the ease of its use. For example, in the case of BTCST, the way token holders can obtain rewards and become stakeholders in the project is easy to understand. The regular distribution of BTCST profits from staking is guaranteed when 60% of the total supply of BTCST has been staked. If less than 60% of the total supply of BTCST is staked in the dApp, the project team would still deposit 60% of net daily mining rewards to the dApp to be shared by the staking participants. These rewards are deposited to valid pledgers on a day-to-day basis.
The early bird gets the worm, and those who have discovered hash rate tokens early have so far achieved good returns. Since its debut on the Binance launch pool, more than US$300 million in returns has been farmed by staking BNB for BTCST. Other than that, miners that obtain and hold BTCST are incentivized to become market makers as well as support the project. This gives miners the opportunity to contribute more to the mining industry than ever before. The added flexibility is an attractive feature as well. For miners, hash rate tokens could be a new way to capture the profits derived from physical mining machines. Other than that, it provides a simple way to transfer hash rates to different mining farms. In terms of risk, hash rate tokens alleviate risks such as costs and downtime caused by force majeure factors such as mining machines being offline for whatever reason. Judging from these factors, there is a good argument for the case of hash rate tokens to be the best method of mining available.
Where do cloud mining platforms fit in this equation?
Cloud mining platforms and the use of mining machines directly compete with hash rate tokens. There is no question that with every emerging cryptocurrency model that arises, there are risks accompanied by the opportunities and potential they bring. Therefore, the possible dangers of hash rate tokens deserve attention.
Lack of transparency in hash rate tokens
Hash rate tokens are distinct from cloud computing systems that guarantee real mining operations. In theory, the hash rate token is pegged to the corresponding computing power and the revenue is divided and given out proportionally by accessing the computing power of the desired mining farm. However, it is uncertain if there is real computational power behind hash rate tokens and whether the project behind the token guarantees equivalent mining machine computing power.
Cloud mining platforms provide services based on real-time monitoring of computing power and scheduled compensation to users. While it may be a stretch to say that all cloud mining services on the market are reliable, the top-tier institutions generally make it a point to make transparency a priority and put the appropriate measures in place. For example, at Bitfufu, a cryptocurrency mining platform, users can track each computing power to the computing power plan that is run by the selected machine, and the platform can be traced back to the computing power package. Mining farms and individual mining machines have real computing power and send data, including mining pool computing power statistics, to the platform interface. In addition, every hash rate consumed in Bitfufu can be tracked and assessed. Mining revenues are calculated by the mining pool, which means that the earnings are derived directly from the pool to its customers. It is worth mentioning that, at present, only Bitfufu and Bitdeer have been able to divide computing power by hash rate (T).
A steady supply of computing power at cloud mining service providers
Cloud mining service providers partner with mining pools and other mining institutions to ensure the stable supply and authenticity of computing power used. Other than this, cloud mining platforms have resources that allow for mining with lower energy consumption ratios, while maintaining higher gains for users. As a one-stop physical mining machine mining platform centered on self-operated mines, Bitfufu contains a range of computing powers from their machines, and these plans have been carefully selected and approved by the platform. Suppliers, therefore, are able to provide transparent, fair, and easy to understand real mining services to customers. The platform dramatically reduces mining costs through economies of scale. At the same time, it has access to high-quality manufacturers worldwide.
The fees required for using a cloud mining service is also not as expensive as it may seem. For instance, mining fees at Bitfufu relatively affordable on the market in terms of computing power cost per terabyte of mining machines and the electricity cost per kWh. In fact, the computing power cost per terabyte at Bitfufu is almost the lowest price available in the industry. Save for an electricity charge of RMB 0.38 per kilowatt-hour, the platform does not charge any additional charges. In this regard, the fees for cloud mining are a small price to pay for peace of mind.
Cloud mining services are more risk-resistant
In terms of risk resistance, cloud computing power much more resistant to risk. Hash rate tokens, as a centralized currency, would suffer a sharp decrease in the price of the token in the event that the token is inflationary. The current market environment for bulls may cover some of these risks, but if the price of bitcoin plummets and mining income falls, the price of hash rate tokens is likely to fall off a cliff.
In contrast, cloud mining platforms are better able to hedge against the risks since the profits can be influenced by other factors outside of the price of the cryptocurrency. Taking Bitfufu and their 30/40/50 series of computing power service plans as an example, the most of energy consumed does not exceed 60W/T and for the 30-series plans, energy consumption ratio can even be as low as 30W/T, which is equal to the that of the current S19Pro model mining machine. It allows for the price of the plans to remain low even when the currency price drops, to mitigate the possible loss in gains. In addition, the energy consumption ratio of the regular hash rate anchored to the BTCST is 60W/J, which is exceedingly high. This means that in the case the price of the currency decreases, the mining revenue may not be sufficient to cover the cost of energy, and because of that, the potential risk is very high.
Cloud mining service providers are becoming more innovative
The hash rate token is indeed a breath of fresh air, but existing cloud mining service platforms are still able to offer novel solutions to the market. Bitfufu has pioneered the standardization of cryptocurrency hash rate. What that means is that multiple models of the same series under Bitfufu are intelligently operated as a unified system to deliver standard power consumption. This mining product is bound to become the industry’s most effective response when it comes to promoting its ongoing development, while at the same time providing more efficient transactions and liquidity.
Even when it comes to the ease of transfer as seen in hash rate tokens, cloud mining services have also begun to offer convenience to their users. For instance, Bitfufu will enable users to transfer their purchased services to other users in January 2021. If the users wish to terminate the service for themselves, it can easily be transferred to other users. In addition, Bitfufu is expected to launch a free transfer of computing power in February 2021 so that users can conveniently trade in computing power.
It is also worth considering, of course, whether other cloud computing power platforms would in the future launch hash rate tokens and compete with projects, all while claiming a higher degree of reliability and security, but this remains to be seen.
Indeed, the emergence of hash rate tokens has provided conventional mining machines and cloud computing platforms some competition. It should be noted that engaging in cryptocurrency mining requires a strong grasp of industry expertise, and it is important to consider the risks behind it. Relatively speaking, cloud computing platforms such as Bitfufu are still the best choice for current mining users after benchmarking other choices in terms of convenience, reliability, and risk tolerance.
Disclaimer: This is a paid post and should not be taken as news/advice.
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