Energy Coaching
I get A LOT of questions about Karma. Loads and loads and loads. I know that a lot of you have been waiting for this post and it seems that today’s the day that you’re finally ready for it (oh, you thought the timing was all MY idea? No, no my pretties. It’s all you. I’m just the happy shiny and willing (not to be taken the wrong way) messenger. So, without further ado, here’s what I have to say about Karma. But, I’m going to warn you now, I feel an acute attack of sarcasm coming on. For those of you who enjoy that sort of thing, you’re welcome.
Does Karma Exist?
Well, that was easy.
Oh, you want more? Ok, fine. I’ll explain.
When people talk about Karma, they usually mean one of two things:
What comes around goes around (i.e. if you hurt someone, something bad will happen to you.)
If something bad happens to you, it’s because you did something horrible in a past life and it’s coming back to bite you in the ass.
These two, frankly bullshit, beliefs are based on two even more bullshit assumptions (oh yeah, there’s going to be cursing in this post, people. I feel strongly about this):
Assumption Number 1: The Cosmic Bank Account
In order for there to be such a thing as Karma, there would have to be judgment, which we know (well, some of us do), is a human concept, not a Universal one. The Universe does not judge you. There is no cosmic moral bank account that keeps track of your actions and intentions from this life or any other, and then seeks to create a balance between the credits (actions judged to be “good”) and debits (actions judged to be “bad”).
First, of all, who could keep track of such a tally? And second of all, who gets to decide which actions go on which side of the balance sheet? Sure, you might say that murder is always bad. But is it? What if it was self defense? What if it was in defense of another? What if the murderer is mentally disabled and had no idea what he was doing? What if it was an accident? What if you lived in an age or area where killing others was a way of life and you learned that it was ok? What if it happens during war? What if you were ordered to do it? Does it make a difference if you know it’s wrong? And we’re just talking about killing here, never mind all the lesser “sins”.
Ok, some might say, the deciding factor isn’t the action, but the intent. If you actually wanted to hurt another being, then you’ve got bad Karma. So… every time you feel powerless about something and it causes you to get angry, and in that anger you want to smack someone, you are adding to your negative balance sheet whether you actually do it or not? In that case, you might as well get to smackin’, you’re already screwed. By the way, can we see where some of the screwed up ideas about negative emotions are coming from?
Assumption Number 2: The Boomerang Effect
Let’s take a look at the idea of “what comes around goes around”. Basically, believers of this adage will tell you that whatever you put out in the Universe comes back to you, kind of like a boomerang. So, if you throw out your boomerang of negative intent, like say, wanting to smack someone (I’ve got a theme going here), you spew forth that energy and after a while, it turns around, comes back to you and smacks you in the face, sometimes literally. But, if you put out a lot of kindness, the energy of that turns around and graces you with . And if you end up losing all your lottery winnings a couple of years later, then the money obviously corrupted you, causing you to create negative Karma, which then came and took all your money.
Why we like Karma
In other words, Karma allows us to explain why bad things happen, and it’s always by assuming that you get what you deserve. When we see something bad happen to someone, we console ourselves with the idea that he must’ve done something to deserve it. He must’ve been a bad person. And well, we’re not bad people, so we’re safe. That thought feels much better than thinking that random shit could just happen to us at any time and there’s nothing we can do about it. Or, to put it more bluntly (and just to amuse myself): We like to think the poop can’t hit us if we didn’t fling it first.
When Karma breaks down
The problem arises when really bad shit happens to really good people. That’s when it gets a bit more depressing. What did they do to deserve this? How could so much pain be showered upon people who have clearly done nothing wrong? It’s easier to use Karma as an excuse when it comes to strangers, but when we know the “victims”, or when bad crap happens to us, the explanation falls short. The best we can come up with then is to speculate that we must’ve been really, really evil in a , which is totally unsatisfying at best.
We’ve always had a need to make sense of . The idea that events are just random didn’t feel good (because it’s not true), so we searched for a better feeling explanation (as is our nature). We came up with Karma (I’m going to skip all the stuff about how religions picked right up on the concept and used it to make us feel guilty just for being born and all that). And well, Karma did seem to explain a lot, and when it didn’t, we could tweak it so it did. But when it didn’t seem to apply, we had to admit that sometimes bad stuff just happened to good people and that there was nothing we could do about it. So, when Karma explained things we could feel a bit better, and when it didn’t, the only other option we had was to feel powerless.
A better explanation
Here’s where LOA comes in. Instead of giving you two options – one really crappy one and one slightly better but flawed one, LOA offers an explanation that, if you accept the premise, makes sense. Every. Time.
(Notice that I said that you have to accept the premise. People who don’t resonate with the basis of the Law of Attraction aren’t going to resonate with this explanation either. Keep that in mind when you go to correct someone who claims that they’ve been divorced three times because of Karma.)
What about when Karma seems to be working?
One of the most frequent questions I get about Karma generally involves the witnessing of how someone did something bad and almost immediately experienced something painful being done to them. The boomerang effect seemed to be working well and to the great delight of the onlookers. How, pray tell, I’m usually asked, do I explain that if there is no such thing as Karma, eh?
Here’s how: It’s called the LAW OF FREAKING ATTRACTION!
So, there’s evil Bob, doing evil things, and BAM something evil is done onto Bob. Let’s look at what really happened, shall we?
Bob is not evil. Bob is doing evil things because Bob is in a great deal of pain and feels totally powerless and being a sadistic asshole is the only way that Bob knows how to make himself feel better. Having control of others, even for a moment, means having control of something. So, Bob does what he can to relieve the suffering he feels in the only way he knows how.
The vibration that Bob is offering is one of powerlessness. Guess what powerlessness attracts? That’s right, experiences that make Bob in other words, experiences of more pain. So, while it may seem that Bob is getting exactly what he deserves, Bob is really getting exactly what he’s attracting. There’s a difference.
Now, take Happy Susie. Happy Susie is happy (hence, the name), and spreads her happiness throughout the kingdom. People are always kind to Susie and seem to just give her stuff. Isn’t that Karma? Well no. It’s energy. Susie is happy. She has a high vibration. She’s going to attract more experiences that match that happiness.
It’s not about what you deserve
It’s not about your intent or your actions. There is no judgment. There is no tally sheet. And, there is no boomerang. When bad things happen to you it’s not to punish you and it’s not because you deserved it. When painful events happen, they usually happen for one of two reasons:
You have massive amounts of resistance, and you’ve had tons of smaller, much less painful manifestations which have been trying to get your attention for eons, but which you’ve ignored. It took something really big to get your attention.
It’s not about you at all, and you’re in pain because the perspective with which you’re looking at the situation is totally messed up (due to how you’ve been taught to look at it).
It is never, ever, EVER because you deserved it. What’s more, you don’t have to prove your worthiness is order to deserve something good.
just so that you can get good Karma points, and you’re not aligning with the energy of whatever it is you want, you’re not going to be reaping any rewards soon. You can’t get in good with the judge if there’s no judge. And, say it with me now, THERE IS NO JUDGE.
Letting the evil bastards off the hook
Here’s another question I get frequently: But what about people who’ve truly done bad things? Shouldn’t there be some kind of universal punishment for them? After all, it feels kind of good when the guy who embezzled millions from old grannies gets cancer of the balls. Can that guy really just repent and/or think positively and wipe the slate clean? (I may have paraphrased a bit, but you get the gist).
Ok, first of all, there’s no slate. I already went over that. And no, he can’t repent, because there’s no one to repent to (no judge, remember?). There’s no absolution because there’s no reason for it. And yes, I know that this is the hardest pill to swallow. The Universe does not judge you. Even if you’re an evil bastard. That’s because the goal is not to prove your worthiness and be the best person you can be, it’s to be the happiest person you can be. And when you’re an evil bastard, you’re not happy, and you’re already punishing yourself by being so far removed from Who You Really Are. You’re already in hell (this is, pretty much, what hell is). What else can the Universe possibly do to you that you aren’t already doing to yourself?
But, can said evil bastard just begin to think positively and manifest loads and loads of happiness? YES! That’s the thing – it is never too late to move towards joy. Not for any of us. No matter how badly you think you’ve messed it up, you can still find your way to Who You Really Are. You get to be happy. All of us do. And if an evil bastard, aka someone in massive amounts of pain, manages to shift all that energy and find their way to Who They Really Are, if that former unhappy bastard manages to find joy, the Universe doesn’t throw down the towel in disgust and yell at the TV about how unfair that is. The Universe rejoices! Just as it rejoices when any of us find our way to higher vibrations.
And yes, it can, theoretically, happen instantly. Practically, it usually takes just a touch longer to let go of that much pain. Moving from evil bastard to joyful saint would be one hell of a . People have done it, but they usually fall into a coma or something and make the shift while less focused in this reality. I’m not saying it can’t be done, I’m just saying it’s a big ass shift. The process is a lot faster when done deliberately, but no matter how much pain someone is in, or how that pain has manifested in their lives (actions are manifestations, too. More on that in an upcoming post), they can always make their way to joy.
So, now it’s your turn. Have my sarcastic rants validated what you already knew deep down? Or, do you believe in Karma? If so, why? (No sarcasm and no judgment, I promise. I’d really like to know.) Share your thoughts in the comments!
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Recent PostsCitation:&Reynaud,&E.&Protein Misfolding and Degenerative Diseases.&Nature Education&3(9):28
An error in protein conformation can lead to disease. What are the genetic and molecular causes for incorrectly formed proteins?
Current advances in medicine and technology are making our lives longer. Sadly, as our life expectancy increases, the chances of getting a degenerative disease like Alzheimer's, Parkinson's, or diabetes also increases. Why is this? As incredible as it might sound, these diseases are caused not by bacteria or viruses but rather by something conceptually quite simple: incorrect protein folding. Introductory biology courses teach us that proteins are essential for the organism because they participate in virtually every process within the cell. Therefore, if their function is impaired, the consequences can be devastating. As we age, mutations and thermodynamics (as well as some external factors) conspire against us, resulting in the misfolding of proteins. How does this happen? What are the genetic and molecular causes for incorrect folding of proteins, and what is their relationship to aging?
Protein Function and Three-Dimensional Structure
Our modern understanding of how proteins function comes from almost 200 years of biochemical studies. Biochemistry is the science that studies the chemical processes in living organisms. Using different experimental models, biochemists demonstrated that most of the cell's chemical reactions and structural components are mediated or supplied by proteins. These experiments revealed that proteins are crucial for proper cell function. Actually the word "protein" comes from the Greek proteios, which means "first" or "foremost," reflecting the importance of these Figure 1:&Proteins are long polymers made of amino acids.(A) Part of the amino acid sequence of a spider silk protein. (B) The three-dimensional configuration of the same protein.© 2010
Askarieh, G. et al. Self-assembly of spider silk proteins is controlled by a pH-sensitive relay. Nature 465, 236&#10). All rights reserved. molecules. In 1917 the German chemist Hermann Staudinger proposed that organic molecules such as proteins were organized in polymers, giant molecules made of small-molecule constituents linked together by chemical bonds in long chains. This idea contradicted the prevailing hypothesis, and it took some years for biochemists to accept it. Today researchers know that proteins are long polymers made out of a set of twenty small constituents called amino acids (Figure 1).
How are proteins made in the cell? The answer to this question took decades of study and the birth of a new scientific discipline: molecular biology. Many experiments had shown that DNA is the vehicle of genetic information, and that DNA contains the information to make proteins. While discovering that DNA is itself a long polymer made out of four different types of small molecules called nucleotides, scientists realized that genetic information is transferred from a language system of four letters (nucleotides) in DNA to a language system of twenty (amino acids) in proteins.
The Energetic Funnel
The structure of a gene is one-dimensional. This means that a linear sequence of nucleotides codes for a specific linear sequence of amino acids linked to each other in a head-to-tail (amino-carboxyl) manner. The process of converting the information contained in the nucleotides to amino acids using the genetic code is called translation. Conceptually, translation "expands" the concentrated single dimension of the genetic code into a fully realized three-dimensional protein structure. From this point of view, DNA and the genome are very similar to a highly compressed digital file, such as an MP3, in which a lot of information is packed very efficiently. How is this possible? The Nobel laureate Christian B. Anfinsen postulated an answer. He proposed that all the information needed for a protein to fold into its three-dimensional conformation is contained in the amino acid sequence.
© 2000
Adapted from Dinner, A. R., et al. Understanding protein folding via free energy surfaces from theory and experiment. Trends in Biochemical Sciences 25, 331&#00). All rights reserved. To test his hypothesis, Anfinsen applied extreme chemical conditions to unfold an enzyme. These extreme conditions were called "denaturing" and were created with substances like urea, which at high concentrations disrupts the noncovale and mercaptoethanol, which reduces disulfide bonds. What happens to a protein exposed to denaturing conditions? As the primary bonds that hold the protein's three-dimensional structure are disrupted, the protein unfolds. Later, after restoring the natural cellular conditions, Anfinsen observed that the enzyme's amino acid structure refolded spontaneously into its original form. He concluded that the native (natural) conformation of a protein occurs because this particular shape is thermodynamically the most stable in the intracellular environment (Anfinsen 1972). That is, like everything else in nature, proteins achieve the lowest energy state possible. In other words, from the physicochemical point of view of a protein, the amino acids pack in such a way that the free energy of the molecule arrives at a minimum.
Amino acids have different side chains (R groups), which give them different properties. Some of these side chains are big, some are small, some are hydrophilic (interact with water), and some are hydrophobic (tend not to interact with water molecules); some are positively charged, and some are negatively charged. In a properly folded protein, hydrophobic amino acid residues are together, shielding each other
hydrophilic residues are exposed on the surface of the protein, interacting with the water of the cytoplasm; and big amino acids make nooks and crannies for small ones. This kind of tight folding and packing minimizes the overall free energy of the protein.
An average protein has about 300 amino acid residues. If we consider that there are twenty different amino acids, the combinatorial number of protein sequences that can be made is by the most conservative calculation, the human body synthesizes at least 30,000 different kinds of proteins. Furthermore, the number of possible minimal-energy configurations of a single protein sequence is also unimaginably enormous, and usually only a few may have normal activity. Surprisingly, newly synthesized proteins usually fold correctly in the appropriate minimal-energy configuration, and thus they are able to do their job correctly.
As Anfinsen demonstrated, the information needed for proteins to fold in their correct minimal-energy configuration is coded in the physicochemical properties of their amino acid sequence. Usually a protein is capable of finding its functional or native state just by itself, in a matter of microseconds. The concept of how proteins explore the enormous structural conformational space is known as . In 1968, Levinthal proposed that a protein folds rapidly because its constituent amino acids interact locally, thus limiting the conformational space that the protein has to explore and forcing the protein to follow a funnel-like energy landscape that allows it to fold into the most stable configuration possible (Figure 2; Levinthal 1968).
Most proteins follow the correct funnel, but some of them have bifurcating pathways that can make them fold in very different but energetically minimal structures, and only one of these is the native conformation (Dill & Chan 1997). In these cases, something must come to their aid, helping them find the correct native form. Amazingly the rescuer is nothing less than a protein itself.
Chaperones
Proteins that have a particularly complicated or unstable conformation sometimes have difficulty achieving their native state. In these cases other, specialized proteins called molecular chaperones help them find their native functional conformation. Molecular chaperones were first mentioned in 1978 by Ron Laskey, who found that nucleoplasmin (a protein found in the nucleus of the cell) is able to bind to histones. Histones are nuclear proteins whose major function is to interact with DNA to form structures known as nucleosomes (Laskey et al. 1978). Laskey observed that nucleoplasmin acted like a chaperone, accompanying and supervising the activity of the histones and preventing inappropriate interactions. Later, John Ellis extended the term chaperone to describe proteins that help other proteins fold or assemble into protein complexes (Ellis 1987). Interestingly, the existence of chaperones implies that some proteins have inherently unstable conformations that can "flip" from a functional minimal-energy state to a state that is nonfunctional or even toxic. Why is the final conformation of a protein so important? The three-dimensional structure of a protein is what allows it to do its work, to connect with reactive sites on other proteins and molecules within the cell. In other words, the multidimensional structure determines the function, and this concept is one of the most fundamental in biology.
Stable and Unstable Proteins
When native folded proteins are synthesized in a healthy cell, usually everything is right and well. However, our genome also codes for proteins that, as mentioned before, are inherently unstable because they have the property of folding in alternative minimal-energy states. Only very few of these alternative structures are functional an the overwhelming majority are useless or even toxic. The functional or native conformation of non-membrane-bound proteins is typically water soluble. Chaperones will help unstable proteins fold correctly, although some proteins misfold anyway. Misfolded proteins (also called toxic conformations) are typically insoluble, and they tend to form long linear or fibrillar aggregates known as amyloid deposits. But how can a protein change so radically by folding differently, if the sequence of amino acids is the same? The answer is in the way the amino acids interact.
Protein Conformation and the Concept of Misfolding
For many proteins, the most prominent structural motif of the functional protein in its native conformation is known as the alpha helix, a right-handed spiral coil (Pauling et al. 1951). When a protein becomes toxic, an extensive conformational change occurs and it acquires a motif known as the beta sheet. Note that the beta sheet conformation also exists in many functional native proteins, such as the immunoglobulins, but the transition from alpha helix to beta sheet is characteristic of amyloid deposits. The abnormal conformational transition from alpha helix to beta sheet exposes hydrophobic amino acid residues and promotes protein aggregation.
As discussed already, misfolded proteins result when a protein follows the wrong folding pathway or energy-minimizing funnel, and misfolding can happen spontaneously. Most of the time, only the native conformation is produced in the cell. But as millions and millions of copies of each protein are made during our lifetimes, sometimes a random event occurs and one of these molecules follows the wrong path, changing into a toxic configuration. This kind of conformational change is most likely to occur in proteins that have repetitive amino acid motifs, s such is the case in Huntington's disease. Remarkably, the toxic configuration is often able to interact with other native copies of the same protein and catalyze their transition into the toxic state. Because of this ability, they are known as infective conformations. The newly made toxic proteins repeat the cycle in a self-sustaining loop, amplifying the toxicity and thus leading to a catastrophic effect that eventually kills the cell or impairs its function. A prime example of proteins that catalyze their own conformational change into the toxic form is the prion proteins, discussed below.
Under normal circumstances, the cell has mechanisms to prevent proteins from folding incorrectly, as well as to get rid of misfolded proteins. Proteins that have problems achieving their native configuration are helped by chaperones to fold properly, using energy from ATP. Chaperones can avoid the conformational change to beta sheet structure and the aggregation of th thus they seem fundamental to the prevention of protein misfolding. Despite chaperone actions, some proteins still misfold, but there is a remedy: The misfolded proteins can be detected by quality-control mechanisms in the cell that tags them to be sent to the cytoplasm, where they will be degraded (Figure 3).
Infectious Proteins
The concept of an infectious protein, or prion, was proposed in the 1960s to explain scrapie infection. Researchers found that the infectious agent that transmits scrapie is resistant to ultraviolet radiation (which typically destroys nucleic acids), and they proposed that this agent was actually protein based (Alper et al. 1967; Griffith 1967). The idea that proteins could be infectious by themselves was highly controversial because it appeared to challenge the central dogma of molecular biology. Eventually Stanley B. Prusiner and his team purified the prion protein responsible for scrapie, and they were able to show that proteins can indeed be infectious (Prusiner 1982). For this work, Prusiner was awarded the Nobel Prize in Physiology or Medicine in 1997. Prions are also responsible for transmissible spongiform encephalopathies, or TSEs, that include infectious diseases such bovine spongiform encephalopathy (mad cow disease), whose infective form can cause Creutzfeldt-Jak and kuru, the only epidemic human prion disease known. In the late 1950s, before the idea of prions was even proposed, an epidemic of the neurodegenerative disease called kuru suggested that proteins could be infectious. Kuru was discovered among populations of the Fore tribe of the eastern highland of Papua New Guinea, and the disease was associated with their cannibalistic funeral practices. With experimental testing, researchers showed that kuru could be infective in chimpanzees after intercerebral inoculation with brain suspension from kuru patients (Gajdusek et al. 1967). Years later, after kuru was recognized as a prion disease, the discovery that in some conditions prions can be infectious across species led to the naming of a similar neurodegenerative disease, Creutzfeldt-Jakob disease. This affliction could be caused by the ingestion of beef containing toxic protein particles. The conformational error in the toxic protein can also be caused by a mutation, thus making the disease familial. Prions are not an exclusive p they also occur naturally in unicellular organisms such as yeast, which therefore have become good experimental models for studying these protein conformational changes.
Misfolded Proteins and Neurodegenerative Diseases
Accumulation of misfolded proteins can cause disease, and unfortunately some of these diseases, known as amyloid diseases, are very common. The most prevalent one is Alzheimer's disease, which affects about 10 percent of the adult population over sixty-five years old in North America. Parkinson's disease and Huntington's disease have similar amyloid origins. These diseases can be sporadic (occurring without any family history) or familial (inherited). Regardless of the type, the risk of getting any of these diseases increases dramatically with age. The mechanistic explanation for this correlation is that as we age (or as a result of mutations), the delicate balance of the synthesis, folding, and degradation of proteins is perturbed, resulting in the production and accumulation of misfolded proteins that form aggregates (Figure 4; Finkel 2005).
Among the environmental factors known to increase the risk of suffering degenerative diseases is exposure to substances that affect the mitochondria, increasing the amount of oxidative damage to proteins. However, it is clear that no single environmental factor determines the onset of these disorders. In addition, there are genetic factors. For example, in the simplest forms of familial Parkinson's disease, mutations are associated with dominant forms of the disease. This means that an individual with a single copy of a defective gene will develop the disease, yet two copies of the defective gene are required for recessive forms of the disease to develop. In the case of Alzheimer's disease, and for other less common neurodegenerative diseases, the genetics can be even more complicated, since different mutations of the same gene and combinations of these mutations may differently affect disease risk (Dobson ; Chiti & Dobson 2006).
Misfolding in Nonneurological Diseases
Protein aggregation diseases are not exclusive to the ce they can also appear in peripheral tissues. In general, the genes and protein products involved in these kinds of diseases are called amyloidogenic. Such diseases include type 2 diabetes, inherited cataracts, some forms of atherosclerosis, hemodialysis-related disorders, and short-chain amyloidosis, among many others. All these diseases have in common the expression of a protein outside its normal context, leading to an irreversible change into a sticky conformation rich in beta sheets that make the protein molecules interact with each other. The general pattern that emerges in all these diseases is an abnormal tendency of proteins to aggregate as a result of misfolding. The aggregation can by protein hyperphosphorylation (a condition where multiple phosphate groups are added to the protein), by prion self-catalytic conformational conversion, or by mutations that make the protein unstable. Aggregation can also be caused by an unregulated or pathological increase in the intracellular concentration of some of these proteins. Such imbalances in protein concentration can be a consequence of mutations such as duplications of the amyloidogenic gene or changes in the protein's amino acid sequence. Imbalances can also be caused by deficiencies in the proteasome, the cellular machinery involved in the degradation of aging proteins. Inhibition of autophagy (a process by which cells engulf themselves) also promotes amyloid aggregation. In addition, some evidence suggests that the severity of these diseases correlates with an increase in oxidative stress, mitochondrial dysfunction, alteration of cytoplasmic membrane permeability, and abnormal calcium concentration (Table 1; Lin & Beal 2006).
Genetic causes
Alzheimer's disease
Gives rise to Aβ, the primary component of senile plaques
Parkinson's disease
PS1 and PS2
A component of γ-secretase, which cleaves APP to yield Aβ
Parkinson's disease
α-Synuclein
The primary component of Lewy bodies
Parkinson's disease
A ubiquitin E3 ligase
Parkinson's disease
Protects the cell against oxidant-induced cell death
Parkinson's disease
A kinase localized to mitochondria. Function unknown. Seems to protect against cell death
Parkinson's disease
A kinase. Function unknown
Parkinson's disease
A serine protease in the mitochondrial intermembrane space. Degrades denatured proteins within mitochondria. Degrades inhibitor of apoptosis proteins and promotes apoptosis if released into the cytosol
Amyotrophic lateral sclerosis
Converts superoxide to hydrogen peroxide. Disease-causing mutations seem to confer a toxic gain of function
Huntington's disease
Huntingtin
Function unknown. Disease-associated mutations produce expanded polyglutamine repeats
Lin, M. T. & Beal, M. F. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443, 787&#06) doi:10.1038/nature05292.
Looking Forward
At the moment there is no treatment for any of the known amyloid diseases. However, there is hope. The increasing knowledge of the causes of amyloid accumulation is beginning to pay off with possible pharmacological treatments. Therapeutic inhibition of precursor protein synthesis is within reach, with the expanding use of RNA interference (RNAi) technologies. Drugs that induce chaperone expression are also being tested, as well as inhibitors that prevent protein hyperphosphorylation. And as the number of known amyloid beta sheet structures grows, scientists have more options to find common structures for the design of specific chemical inhibitors of aggregation. Finally, vaccines against the aggregates are being developed (Chiti & Dobson 2006). Although we are at risk of accumulating misfolded proteins every day we age, and to function properly our cells must continually make proteins, understanding misfolding will ultimately help protect us from serious diseases.
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