There are 2 types of day traders: institutional and retail. Both institutional and retail day traders are described as speculators, as opposed to investors.
Institutional day traders work for financial institutions and have certain advantages over retail traders due to their access to more resources, tools, equipment, large amounts of capital and leverage, large availability of fresh fund inflows to trade continuously on the markets
In the past, most day traders were institutional traders due to the advantages they had over retail traders. However, since the technology boom in the second half of the 1990s, advances in personal computing and communications technology, realized in the accessibility of powerful personal computers and the Internet, have brought fast online trading and powerful market analytical tools to the mainstream. Low, affordable commissions from discount brokers as well as regulation improvements in favor of retail traders have also helped level the trading playing field, making success as a retail trader a possibility for many and a reality for some.
There are 2 types of day traders: institutional and retail. Both institutional and retail day traders are described as speculators, as opposed to investors.
Institutional day traders work for financial institutions and have certain advantages over retail traders due to their access to more resources, tools, equipment, large amounts of capital and leverage, large availability of fresh fund inflows to trade continuously on the markets, dedicated and direct lines to data centers and exchanges, expensive and high-end trading and analytical software, support teams to help and more. These advantages give them certain edges over retail day traders.
Retail day traders work for themselves, or in partnership with a few other traders. Retail traders generally trade with their own capital, though they may also trade with other people’s money. Laws may restrict the amount of other people’s money a retail trader can manage. In the United States, day traders may not advertise as advisors or financial managers. Although not required, nearly all retail day traders use direct access brokers as they offer the fastest order entry to the exchanges, as well as superior software trading platforms.
Auto traders auto-trade, which stands for automated trading and the use of computer programs and other tools to enter trading orders. Because this all happens with the help of the computer algorithm it is also called algorithmic trading.
Over and over I’ve been hearing stories regarding people going to body mod artists who then sterilize a magnet using an autoclave. This is NOT an appropriate method. It will decrease the strength of the magnet significantly. Furthermore, different materials expand and contract to a different degree under heat. Autoclaving will crack the biocoating for the majority of coating types available rendering the magnet unsafe for implant.
Unless you’re purchasing a presterilized unit, chemical sterilization is the route to go. SFM has done a lot of work on this recently. We’ve tested methods for the Dangerous Things M31, Parylene C, and Silicone. Chemical sterilization IS NOT the same as disinfection or antisepsis. Furthermore, the most common agents such as sodium hypochlorite or hydrogen peroxide will dissolve metal. An M31 in either bleach or high concentration peroxide turns into a nasty black goo. So far, we’ve found the best results with Glutaraldehyde. I’m going to be writing up our results in the next AugLim post which should be out in a week.
Parylene C has so far held up well to the majority of the above chemicals but we didn’t use very many samples and found a couple of duds… they had preexisting cracks. I’m not sure why this is so. SovereignBleak for example has had a Parylene C coated magnet in for years. I’ve had a V&P for at least 3 now with no problem. There may be serious differences in quality based on the place performing the coating.
Silicone bleaches white and has some changes in texture. I can’t say how this would affect an implant overall, but I’d be concerned.
Like I said, I’ll provide a lot more info in the post but I thought this important enough to get out into the forum now.
So I’ve been wondering about conditions that might demagnetize an implant. Are there any known conditions or circumstances that could endanger the magnetic properties of the implant that wouldn’t also damage/destroy the hand it’s implanted in? Has anyone here ever had an implant be demagnetized while it was implanted in the body?
Everything I’ve read seems to indicate that neodymium magnets are very hard to demagnetize, but I’ve got this old CRT degausser that I’m dying to plug in and toy with. Could it degauss my implants?
Solution Structure of C-terminal AbrB
NMR structure of the catalytic domain of the large serine resolvase TnpX
As of Tuesday Nov 25, 2014 at 4 PM PST there are 105212 Structures.
New Structure ID List:
[2MHC, 2MJG, 2ML9, 2MM5, 2MM6, 2MPO, 2MT6, 2MTO, 2MTT, 2MTU, 2MTV, 2MVX, 2RUM, 2RUN, 2RUO, 3J7E, 3J7G, 3J8G, 3WP3, 3WQQ, 3WQR, 3WQS, 3WSP, 3WT1, 3WT2, 3WZL, 3WZM, 4CDS, 4CDZ, 4CE0, 4CF3, 4CF4, 4CF5, 4CJD, 4CLQ, 4CMY, 4CP8, 4CQI, 4D6C, 4D6D, 4D6E, 4D6F, 4D6G, 4D6H, 4D6I, 4D6J, 4KOE, 4KPE, 4KPF, 4KUK, 4KUO, 4KWX, 4N79, 4N8W, 4NI8, 4NKN, 4NKR, 4NNO, 4NQ4, 4NQ5, 4NQ6, 4NQ7, 4NQG, 4NQZ, 4NR0, 4NZ5, 4O1G, 4O1L, 4OB0, 4OB1, 4OB2, 4OB3, 4OBD, 4OBF, 4OBG, 4OBH, 4OBJ, 4OBK, 4OF9, 4OMA, 4ONT, 4OOD, 4P5W, 4P5X, 4P60, 4P9C, 4P9D, 4P9E, 4PF3, 4PG0, 4PH9, 4PHT, 4PVV, 4PWE, 4PWF, 4PWG, 4PWH, 4PWI, 4PWJ, 4PWK, 4PZP, 4Q5V, 4Q6D, 4Q6E, 4QCL, 4QLE, 4QLF, 4QLG, 4QM8, 4QMA, 4QR0, 4QR1, 4QR2, 4QRF, 4QWW, 4R3Q, 4RAW, 4RBP, 4RBS, 4RCK, 4REV, 4RJ3, 4RJ4, 4RJ5, 4RJ6, 4RJ7, 4RJ8, 4RKB, 4RKL, 4RLV, 4RLY, 4RN3, 4RNL, 4RNS, 4RP3, 4RP4, 4RP5, 4RPN, 4RPO, 4RQA, 4RQB, 4RU0, 4TO8, 4TTB, 4TTC, 4TU7, 4TU8, 4TU9, 4TW6, 4TW7, 4TW8, 4TYP, 4TYQ, 4TYT, 4U14, 4U15, 4U16, 4U92, 4UBG, 4ULX, 4UM4, 4UUG, 4UVR, 4UWF, 4UWG, 4UWH, 4UWK, 4UWL, 4V2W, 4W5H, 4W5J, 4W7T, 4W97, 4WHZ, 4WJG, 4WK1, 4WK3, 4WNQ, 4WO4, 4WOK, 4WSI, 4WUI, 4WUR, 4WUV, 4WWH, 4WWL, 4WXE, 4WXT, 4WY2, 4WYV]
In my other thread, I noted that I had problems with my scalpel-based implantation of three m31s (combination of genuine rejection and in at least one case, perhaps my own over-concern leading me to remove it when it might not have been necessary).
15 days ago, I implanted in my middle finger using a needle and about 30 minutes ago, used the same method to implant in the ulnar nerve section of my ring finger. It worked so well the first time that I simply repeated the process for the second installation.
I used the needle of an RFID injector (and if someone could clarify, what is the diameter on the needle used in those injectors? Is it a gauge 10 needle?) Here’s my procedure:
- The entire hand was cleaned with chlorhexadine glucanate (scrubbed for two minutes) then rinsed with saline.
- A hair rubberband was placed around the base of the finger as a tourniquet, after which I used my right hand to force all the blood out of the finger.
- Injector from my xNTi kit was used to make the hole (it was sterilized with chlorhexadine as I’d used it previously to install the chip). There’ll be a picture at the end of this post with the needle in the finger to show the insertion point and path of the needle. I will say that I found it to be pretty damned painful (I’ve had nightmares about it since I first did it, if that tells you anything). This is a big needle to insert into a finger.
- As this hole is a little smaller than the m31, popping the magnet into the hole requires a bit of force. After it was through the entry point, I used the tine of a plastic fork to push the magnet to the very end of the needle hole (I’m inclined to refer to it as the “needle well” in my head for some reason). The fork tine had been soaked in chorhexadine then rinsed in saline.
- The site was wrapped in gauze and taped and the tourniquet removed.
- The following day, I unwrapped the finger, cleaned it with saline, and rebandaged. By this point, the finger was very bruised but almost without pain. It had bled extensively inside the gauze overnight but it was no longer bleeding by the time I unwrapped it. This second one I’ve done this way seems to be bleeding quite alot more, with blood soaking all the way through the gauze within the first minute or two.
- Twice a day for the first week I rinsed the site with saline. I made sure to keep it dry other than that (by the way, those little finger condom things you can buy are fantastic for use while showering). By the third day I was using a basic band-aid rather than gauze.
- The path that the needle took remains visible below the skin even 15 days out. The bruising diminished rapidly over the course of the first week. The site was healed shut inside the first week though it took 12 days for the scab to come off naturally. There is some numbness directly over the site, though the affected area is getting smaller by the day and I expect all feeling to return with time.
- EM sensitivity seems wonderful and quite honestly is a constant source of fascination and wonderment to me.
Regarding why I chose this particular path for the needle, it was for two reasons. Firstly, natural walking movements keep the magnet at the bottom of the hole during healing. Secondly, I’ve made it a habit to shake the hand periodically, which also helps force the magnet to stay at the bottom of the hole.
I’ve seen very little in the way of instructions for needle-based insertions so I hope someone finds this useful. I’ve got one 99% healed magnet and one that was done just this evening using this technique and I can say that it worked very well for me.
Oh, almost forgot the picture. This is my ring finger with the needle at full depth (sorry for the poor quality; its hard to take a picture and keep things sterile at the same time :P):
Extremophiles may be an untapped source of antibacterial drugs<br>Extremophile microorganisms such as those that live around deep sea hydrothermal vents may be a new, untapped source for antibacterial drugs.
Instamorph, Polymorph etc. are PCL based plastics and should (in theory) be able to be used in bioproofing applications I was curious if anyone in the community has actually experimented with this and if so what were the results?
My assumption is that it would be similar to the “hot glue method” but with more consistency as they are generally pure PCL. If no-one else has experimented with this material I’ll give it a try and let you know.
As mentioned in another thread, I’m building a new reader for the biothem chip (yes, I created a new account, I decided I should use my name rather than a handle if I’m going to be selling stuff), since the only current readers are very animal oriented and not ideal when using the chip in humans.
The current system I’ve designed consists of a coil antenna, an RFID decoder chip, an arduino nano, a bluetooth module and a battery. also an android app for viewing the data and configuring the reader.
Since I figure there will probably be at least a few people who want this system, I should ask exactly what people would like to see in the final design.
Feel free to suggest anything, but things I’m particularly interested in hearing about are:
case shape/design. currently the plan is to 3d print cases. right now I’m just dealing with a flat-ish rectangle, with slots on two sides where a strap can be fitted to hold the reader in place on an arm or leg. any suggestions?
battery life/size/shape/weight. naturally longer run time is better, but having a larger battery costs more, takes more space and is heavier. what trade off do people want? one thing to point out is there are two modes of operation: 1) only read the temperature when the user presses a button, 2) read the temperature every few seconds/minutes (as configured by the user), the more frequently you read the temperature, the more power is used. personally I feel it would be good to run for around 12 hours, while reading once a minute, but that requires a reasonably large battery. thoughts?
other possibilities which might be cool, but may make the system cost more, for now I’m not planning to include these features, but if there is enough interest I will, and for software features I can add them later if people want them.
standalone mode: rather than only sending the data to a smartphone, the reader could have added storage to save values read, and transmit them in bulk later.
apps for other OSes: right now I’m only working on android, but I could build apps for iOS/windows/linux etc. apps are free, but I’ll need to change more for the reader to account for the time for me to build each app. I will opensource the android app, so if you’d rather, you can port it to other devices yourself.
built in display: currently the only way to view the temperature value is on the smartphone, I could add a small display to the reader to allow reading value without needing a smartphone.
more ways to export data: currently the app lets you view temperature values, save them to a file and send them in an email. I could add things like facebook sharing etc. personally I don’t want that kind of feature, but maybe other people do?
depending on which features we go with, I’m hoping to keep the price at no more than $100, but if people want every possible feature, it will cost more.
This is your chance to choose the reader design, tell me what you want and I’ll try to make it happen
Solution structure of Blo t 19, a minor dust mite allergen from Blomia tropicalis
Solution structure of opa60 from n. gonorrhoeae
As of Tuesday Nov 18, 2014 at 4 PM PST there are 105025 Structures.
New Structure ID List:
[2MAF, 2MFJ, 2MFK, 2MH7, 2MJD, 2MJE, 2MKM, 2MKO, 2MLM, 3WBI, 3WBJ, 3WBK, 3WMH, 3WMI, 3WMJ, 3WN5, 3WVQ, 3WVR, 3WWL, 3WWM, 3WWN, 3WYK, 3WYL, 3WYM, 3WYO, 3WZ1, 4CE6, 4CLC, 4CS1, 4D69, 4KRZ, 4KS0, 4KXK, 4KYO, 4LY7, 4NEJ, 4NEM, 4NG6, 4NHK, 4NHL, 4NHM, 4NHX, 4NHY, 4NKE, 4NKF, 4NL0, 4NLF, 4NMG, 4NMJ, 4NMK, 4NND, 4NNS, 4NNT, 4NNX, 4NNY, 4NO0, 4NO2, 4NOA, 4NRR, 4NRS, 4NUA, 4NXY, 4NZS, 4OAY, 4OAZ, 4OB4, 4OFC, 4OMW, 4OMX, 4P7E, 4PED, 4PFZ, 4PG1, 4PNO, 4PVA, 4PVO, 4PVT, 4Q2C, 4Q2D, 4QBA, 4QCC, 4QGO, 4QH0, 4QII, 4QIJ, 4QM9, 4QUZ, 4QV2, 4QVA, 4QVJ, 4R3E, 4R3F, 4R4C, 4R4I, 4R4O, 4R4Q, 4R4T, 4R81, 4R9U, 4RCA, 4RCM, 4RCW, 4RDU, 4RE1, 4RK4, 4RKV, 4RL0, 4RL2, 4RM5, 4RMF, 4RNE, 4RNF, 4RNG, 4RNH, 4RNI, 4RNJ, 4RNR, 4RO6, 4RQO, 4RQQ, 4RS2, 4RS3, 4RSH, 4TRK, 4TZJ, 4TZL, 4TZM, 4TZN, 4TZO, 4TZQ, 4TZS, 4U0T, 4U0X, 4U4S, 4U4X, 4U5Y, 4U93, 4UMX, 4UMY, 4UYN, 4UZD, 4UZH, 4V0K, 4V0L, 4V0M, 4V0N, 4V0O, 4WGI, 4WJS, 4WJU, 4WJV, 4WK5, 4WP0, 4WQN, 4WRT, 4WSA, 4WSB, 4WSH, 4WUN, 4WUZ]
This is a tangent that popped into my head that could be a viable project for us due to it’s simplicity. Concept is simple. Modify readily availiable probiotic bacteria to contain genes that allow them to produce the vitamins that we currently have to ingest. They would have to be able to break down and process our waste and turn it into vitamins. This is already done for vitamin k (i think, this is off memory, but i know one of our vitamins comes from out gut). So why not all the rest? no more supplements and it could even work as a treatment for those deficient in one vitamin or another. Hell we could even have one produce massive amounts of vitamin A1 from glims and cassox vision trial. Sure it won’t give you super vision but it could be interesting to see what your body does with more of it than usual. Possibilities are endless. So thorugh out some ideas and lets get tinkering. I should mention as the lab gets built and funded and such, if any of the ideas put forth in this thread are interesting or well put together I will actually make the bacteria and could run trials with them. SO lets do this!
Ok so there’s been bits of talk here and there about gene doping and some gene projects but I feel it’s time we give one a shot. The idea is fairly simple. See if we can down-regulate myostatin via rna interference or other fairly harmless methods. I’d rather avoid viral vectors for now as they are tricky and permanant. I want this to be a temporary thing. Something that will interfere with the genetic pathways for a short while and then eventually either be broken down or be treatable with a counter agents to turn it off. I felt like rna interference would be ideal as you could use a small dosage so the affect could be fairly localized as once the rna is in use it shouldn’t move anywhere. Or a larger dose could spread but eventually be broken down and allow normal function again.
That’s the plan. Thoughts?
A bird’s-eye view of the protein universe <br>How exactly did proteins first come to be? Do they all share a single common ancestor? Or did proteins evolve from many different origins?
Scientists uncover mechanism that controls the fitness of cells, affecting aging and disease<br>A novel looping mechanism that involves the end caps of DNA may help explain the aging of cells and how they initiate and transmit disease, according to new research from UT Southwestern Medical Center cell biologists.
So, I have been looking into the magnet implants and noticed many folks with them go all jedi when holding out their hands. So, I wanted to ask: Is the sensation limited to the finger tip? Also, is the intensity related to magnet size? The reason i ask is that i wonder if an array of tiny magnets (about 4x3x1 mm) with a hole for fibrous tissue to hold on to would be worthwhile. Placements would be the tips of each finger, between each knuckle (3 for each finger total, two for the thumb), one in the palm under each 1st knuckle, and 4 in an arch shape at thr base of the palm near the wrist.
Amino acid sequence and environment are the most important factors determining the structure, stability and dynamics of proteins. To evaluate their roles in the process of folding, we studied a retroversion of the well-described Trp-cage miniprotein in water and 2,2,2-trifluoroethanol (TFE) solution. We show, by circular dichroism spectroscopy and nuclear magnetic resonance (NMR) measurement, that the molecule has no stable structure under conditions in which the Trp-cage is folded. A detectable stable structure of the retro Trp-cage, with the architecture similar to that of the original Trp-cage, is established only upon addition of TFE to 30% of the total solvent volume. The retro Trp-cage structure shows a completely different pattern of stabilizing contacts between amino acid residues, involving the guanidinium group of arginine and the aromatic group of tryptophan. The commonly used online prediction methods for protein and peptide structures Robetta and PEP-FOLD failed to predict that the retro Trp-cage is unstructured under default prediction conditions. On the other hand, both methods provided structures with a fold similar to those of the experimentally determined NMR structure in water/TFE but with different contacts between amino acids.
Head-to-tail backbone cyclization of proteins is a widely used approach for the improvement of protein stability. One way to obtain cyclic proteins via recombinant expression makes use of engineered Intein tags, which are self-cleaving protein domains. In this approach, pH-induced self-cleavage of the N-terminal Intein tag generates an N-terminal cysteine residue at the target protein, which then attacks in an intramolecular reaction the C-terminal thioester formed by the second C-terminal Intein tag resulting in the release of the cyclic target protein. In the current work we aimed to produce a cyclic analog of the small -Ec-1 domain of the wheat metallothionein, which contains six cysteine residues. During the purification process we faced several challenges, among them premature cleavage of one or the other Intein tag resulting in decreasing yields and contamination with linear species. To improve efficiency of the system we applied a number of optimizations such as the introduction of a Tobacco etch virus cleavage site and an additional poly-histidine tag. Our efforts resulted in the production of a cyclic protein in moderate yields without any contamination with linear protein species.
Aggregation of the protein α-synuclein (α-syn) has been implicated in Parkinson’s disease and other neurodegenerative disorders, collectively referred to as synucleinopathies. The β-wrapin AS69 is a small engineered binding protein to α-syn that stabilizes a β-hairpin conformation of monomeric α-syn and inhibits α-syn aggregation at substoichiometric concentrations. AS69 is a homodimer whose subunits are linked via a disulfide bridge between their single cysteine residues, Cys-28. Here we show that expression of a functional dimer as a single polypeptide chain is achievable by head-to-tail linkage of AS69 subunits. Choice of a suitable linker is essential for construction of head-to-tail dimers that exhibit undiminished α-syn affinity compared with the solely disulfide-linked dimer. We characterize AS69-GS3, a head-to-tail dimer with a glycine-serine-rich linker, under oxidized and reduced conditions in order to evaluate the impact of the Cys28-disulfide bond on structure, stability and α-syn binding. Formation of the disulfide bond causes compaction of AS69-GS3, increases its thermostability, and is a prerequisite for high-affinity binding to α-syn. Comparison of AS69-GS3 and AS69 demonstrates that head-to-tail linkage promotes α-syn binding by affording accelerated disulfide bond formation.