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molecular chaperones

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Proteins consist of a set of Piau small molecules known as amino acids, a specific sequence of amino acids will ensure that the future can take a specific protein structure and function. The assemblage of various amino acids is carried out by molecular complexes known as ribosomes, the amino acid sequence formed proteins, however, are synthesized in the ribosomes simply linking to one another in sequence the various amino acids and thus initially consist of chains without a precise three-dimensional shape. Most of the protein chain wraps then spontaneously to take the final structure, the proteins tend to fold in such a way as to avoid ch nonpolar side chains of amino acids come into contact with the aqueous environment of the cell. Not all Portein can fold spontaneously, some are made up of hundreds of amino acids and must be helped to fold properly. the specific sequence of amino acids as we said it is important to allow the protena to fold into a specific shape and could take a specific functionality. If the withdrawal is not successful the feature is missing, or can be modified with deleterious consequences for the cell.




Cells can not wait passively proteins ripieghino correctly. Proteins are often incorrectly wrapped in apolar amino acids on the surface, rather than hidden in a safe in them. These non-polar hydrocarbon portions bind strongly with similar portions on other proteins and forming large aggregates. Random aggregates leading to the death cells: diseases such as sickle cell disease, mad cow disease, and Alzheimer's disease are caused by unnatural combinations of proteins that form fibrils which interfere with the cellular life.
Fortunately, the cell takes care of everything and there is a particular protein known as grppo Chaperon that guide other proteins during the process of proper folding. Protect them during the retreat shielded by other proteins that may bind and prevent the process. Many chaperone proteins are called "thermal shock" (with names such as HSP-60) because they are synthesized in large amounts when cells are exposed to strong heat, as in the case of burns. Too hot in general, destabilizes the protein and makes folding more often wrong. So when the temperature rises too much, the cells need extra help with their proteins.


The Chaperon HSP-60
This type of chaperone is complex and creates a closed environment for protein folding during which protects them completely during the process. An example is the complex GroEL- GroES of E.coli bacteria.
The structure consists of two overlapping rings of GroEL proteins, colored in green and blue, and a cap on the underside of GroES protein, colored red and yellow. As shown in the picture above, seven GroEL proteins form a ring with an internal cavity of the size of a protein. Proteins do not come wrapped up in this cavity and fold in it.

The Chaperon and HSP-70 chaperone prefoldin

Some smaller proteins that protect the ribosome have just left. At this stage the protein can have a very small percentage of their structure already folded, so the portions of the elongated chain with groups of non-polar hydrocarbon type are particularly susceptible to aggregation.

The chaperone HSP-70 (shown above) these portions is elongated, and there binds the fencing from the surrounding molecules. Then, with the energy of ATP, the chaperones release the chain when it is ready to fold. The HSP-70 are composed of two domains: one that binds ATP and controls the process, shown in the upper left from PDB 1dkg, and one that binds to portions of the protein chain is not wrapped in apolar hydrocarbon groups. A small peptide, colored pink, is tied in the deep cleft that binds the protein.

explore the structure

The large complex GroEL-GroES. In this figure three subunits have been removed GroEL in each ring to show the interior, leaving four subunits in each ring. In the two subunits on the back, hydrocarbon nonpolar amino acids LEU, ILE, VAL, MET, PHE, TYR and TRP are colored in blue. Note the strip of hydrocarbon hydrophobic amino acids near the entrance at the top. This interacts strongly with proteins do not fold luring them into the cavity. Now look at the lower cavity, capped by GroES in the bottom colored red. Using the energy of ATP (ADP is located in this structure, colored in red), the ring GroEL undergoes a great change in shape. The cavity becomes much larger, and the strip of hydrocarbon nonpolar amino acids is no longer in contact with the cavity. This means that a protein chain trapped inside (not shown) to close in on itself, having enough space for the process.

Sources:

PDB

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THE CARNIVAL OF BIODIVERSITY '

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In life it takes courage

I learned to forgive, I have been able to go ahead, bite the bullet and be optimistic . I was haughty and proud at the right time and I was detained from making havoc of my dignity. When it came time to open my heart to a certain person, despite the idea terrified me , I gave free access to all my most intimate thoughts, without hiding or concealing anything. I was myself. I was vulnerable , because it would be just a simple word to destroy my protection, the force that even when I was immersed in the frustration and suffering could make sense of the struggle that I was fighting, a silent battle against myself, against my fears, against the world, against love, but above all against all rational behavior . A choice that they had all despised, seeing it as completely insane and wrong, has proved over time that the only ricucisse to sew the wounds that I wore on the heart. Today, thinking back to how I reacted in that situation, I can not help but be proud me and see how the courage, sensitivity and patience before or then always reward those who know how to use them in the right dose.

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The bacterium that utilizes the topoisomerase

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Here, the image on the right, the bacterium that if he had done so much talk in recent days. First, it must be said that all bodies to function properly, they must continually build new components for mobiles and it must be provided with a specific group of items. They are also known as macro-or macronutrients, because micro-organisms, but is also true of us, really in need in high quantities, are the elements that make possible the synthesis of carbohydrates, lipids, proteins, nucleic acids, etc. ... the elements are carbon (C), hydrogen (H), nitrogen (N), oxygen (O), sulfur (S), phosphorus (P). There are others, mostly ions, but these six elements are the skeleton of all organic molecules. Through this discovery, scientists say, although these elements are the building blocks of matter living, it is theoretically possible that other elements that we find on the periodic table can be effectively used in the same way.

The bacterium in question is a strain of gammaproteobacteria (GFAJ -1) which belongs to the family of Halomonadaceae. not yet understood because the microorganisms have a soft spot for arsenic. Evidently he has adapted to live in an environment where the presence of 'arsenic was very high, and therefore has learned to exploit both phosphorus and arsenic, but is yet to be proven. Oremland co-author of the discovery had already observed in the past that the bacteria in the lake, Mono Lake, full of arsenic, typically using this highly toxic reactions in photosynthesis, but no one had demonstrated the absorption of this element for internal use.

Wolfe-Simon and colleagues have collected mud and other sediments from Mono Lake and the bacteria have grown in the laboratory have taken then performed a series of dilutions intended to replace any remaining phosphate solution with higher and higher amounts of arsenic. They found that a type of microbe in the mix seemed grow faster than others.

They then radioactively labeled arsenate which was added in the culture medium so as to be able to monitor its distribution, it was observed that arsenic was present in the bacterium and was contained in proteins, lipids and metabolites such as ATP and glucose, as well as in nucleic acids that made up his DNA and RNA. The amounts of arsenic found were similar to those expected for the phosphate in normal cells, suggesting that the compound was used in the same way they would normally use the phosphate in the cell.

The team used two different techniques of mass spectrometry to confirm that the DNA of the bacterium contained arsenic, indicating that the item had assumed the role of phosphate in holding together the backbone of DNA. Further investigation have confirmed that the arsenate ion PERFORMED bonds with the carbon and oxygen in much the same way as the phosphate.

Now there are a number of questions you will answer. For example, if the phosphate content in kind as the ATP molecule was exchanged with arsenate, what effect it has on fnzioni important turning point in the cell? How can it be just as efficient? Metabolic processes in which arsenic would bind with glucose, if it is known that arsenic is more unstable in contributing to the formation of organic molecules, as it may be equally or similarly effective? And the phosphate groups bind to proteins and which play an important role in those changes of structure features of the latter? how can the exercise arsenate able to work effectively similmete? arsenate ion in fact similar in shape to the phosphate ion form bonds much weaker in water than those formed by the phosphate, is unstable, this means that they tend to break away and even though there may be other molecules that help stabilize these ties, the researchers would need to explain this discrepancy in the event standing. Yet, the discovery is "simply phenomenal" if you stand up after further chemical analysis, Benner added: "

means that many, many things are wrong in terms of how we see the molecules in the biological system."

SOURCES:

Nature, Scientific American , EurekAlert

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BIODIVERSITY '

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Fever

When the cold became slightly more pungent, like every year, I made an annoying cold. Apart from that everything runs as usual, there are the usual family quarrels and unnecessary school is pretty good. It is a time that I feel a bit 'lost , a bit' lost in all my conflicting thoughts and I would need even more cuddles and affection. I happen to think about the past and experience a 'distress devastating, but if I think about the future I can not imagine anything. Dark, full vacuum . I hope that my paranoia is exaggerated quest'accentuazione only due to fever and to pass soon.

{ And I find it kind of funny, I find it kind of sad The Dreams In Which I'm dying are the best I've ever had. I find it hard to tell you, I find it hard to take When people run in circles it's a very very mad world / / Mad World - Gary Jules ♪ }

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Neuraminidase

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The flu virus is constantly evolving, every year we hear of new strains, in fact, every decade or so, a new strain is dangerous and poses a threat to public health. Last year, there was an outbreak of a new strain of flu virus, the '
H1N1, more commonly known as swine flu virus. The name H1N1 refers to two types of molecules that coat the surface of the virus: hemagglutinin
and neuraminidase . Together, these two molecules determines the infectivity of the virus. The hemagglutinin plays a decisive role when the virus approaches the cell by binding to the polysaccharide chains on the cell surface and then injecting the
viral DNA into the cell. The neuraminidase, on the other hand, comes into play when the virus leaves the infected cells. Ensures that the virus does not remain bound to the surface polysaccharides of cutting their chains.

Cut sugars

The neuraminidase, shown above from the PDB file 1nn2, consists of four identical subunits arranged a square. It is normally linked to the virus surface protein with a long arm, not shown. The active sites are located in deep depressions of the surface above, bind to cellular polysaccharide chains and cut the sugar terminal. The surface of the neuraminidase has linked some of the chains of polysaccharides in the structure above, we see extend upwards and downwards, and are similar to the polysaccharide chains present on the surface proteins of our cells.

Pigs and people

As the hemagglutinin, neuraminidase, even if there are several sittotipi known as N1-N9. These subtypes are defined by their interaction with antibodies: all variants of the same subtype are neutralized by the same type of antibodies. These subtypes are one of the causes of the continued aggression of influenza. Some subtypes can infect people, infect other birds and others can attack the pigs or other mammals. When different viruses infect the same body, the various subtypes can be mixed and combined in different ways, giving rise to new random combinations that occasionally can be particularly dangerous or even fatal, thus leading to the formation of new strains

. fight the flu are two most effective drugs currently in use to fight the flu: zanamivir (Relenza) and oseltamivir (Tamiflu). These drugs have been discovered using crystal structures taken from PDB files. By studying the binding of various molecules with the active site of neuraminidase, the researchers were able to design new drugs that mimic the natural substrates of the enzyme. These molecules bind strongly in the active site and block the action that is essential for the release of virus from the cell membrane. Here are shown two structures of these drugs. the middle, PDB file 3b7e, zanamivir is shown (blue) linked to the English influenza virus neuraminidase that caused a pandemic in 1918. Below, PDB file 2hu4, oseltamivir is shown (blue) linked to the avian influenza virus neuraminidase.

Antibodies and vaccines When we get sick of influence, our immune system produces antibodies to fight the virus.
An influenza vaccine can prepare your immune system for this protective action by putting it in contact with a weakened virus or harmless fragments of the virus. In this way the vaccine makes the immune system to produce the right antibodies before infection occurs itself. antibodies recognize proteins on the surface of the virus. antibodies most effective are those that attack the hemagglutinin and thus block the infection of new cells.
antibodies against neuraminidase, such as those shown here in blue, the image comes from the PDB file 1NCA can make it lighter than the flu, and they too help to fight the virus.

explore the structure
To design a drug that could cure people should pay close attention. drugs should be different from the natural substrate of the enzyme so that the enzyme can not catalyze the reaction to destroy them. the same time, the drugs must be very similar to the natural substrate of the enzyme to bind strongly to the active site to block it. It 'also important that medications are similar to natural substrates to avoid drug resistance. An example of this problem is illustrated in three figures below The first figure shows the neuraminidase bound sialic acid in its active site, PDB file
2bat
. This figure shows the normal interaction of the enzyme with a polysaccharide, its natural substrate. The second figure shows the link with oseltamivir, a drug used to combat influenza, 2hu4 PDB file. Note that this is similar but not identical sialic acid. E 'slightly larger forces and a glutamic acid (pink) to bend a little' to the histidine on him (also pink). The third figure shows a variant of the enzyme who developed drug resistance, 3cl0 PDB file. In this mutant enzyme, histidine has been replaced by a tyrosine (Tyr274 pink), being larger, glutamic acid leads down to the drug. Oseltamivir can still bind, but in a less strong due to interference with glutamic acid (pink) and thus can be ousted out of the polysaccharide, the natural substrate. The drug is therefore ineffective in combating the virus mutant. However, there is still enough space to bind sialic acid, and then the mutant enzyme still functions to perform its normal action release of the virus.

Sources:
PDB

Concord Vampiro Cleats

haemagglutinin


var _gaq _gaq = genome consists of single-stranded RNA mold. Virulence of influenza there are three main types, named A, B, C. The main difference lies in the proteins of the major capsid nucleocapside.Le caratteistiche conferitici are two proteins found in extensions known as the spike protein. One is called hemagglutinin, the other neuraminidase. The first is also the rincpale protein on the surface of the virus, is also the main site of AACC by antibodies. It is also the protein that shows increased genetic drift, and it is precisely the root cause of the continuing development of new strains, so every year we end up with new vaccines.


The influenza virus is a dangerous enemy. Normally the immune system fights viral infections by killing the virus for several days and causing the annoying symptoms of influenza. Each year, influenza vaccines activate the immune system to enable it to fight the most common flu viruses. About every twenty years, it appears that a new flu strain is much more virulent than those pitches, and then spread with great rapidity. This happened, for example, at the end of World War causing a pandemic (known as English), which has killed more than 20 million people, more than twice as many people who were death in war.


Hook the target and attack
The hemagglutinin is one of the factors that make the virus so effective. It 's a tip-shaped protein that extends out from the surface of the virus. In the active form shown here, 1ruz PDB file, the hemagglutinin consists of two different types of chains shown in blue and beige. The chains are blue the latching mechanism of the target, looking for particular sugar chains on the cell surface. When found, the hemagglutinin binds to, thus engaging the virus to the cell, then the chains beige begin the attack, as shown on the next page. The name

hemagglutinin refers to the ability of influenza virus to agglutinate red blood cells: the virus is covered with several hemagglutinin molecules that can bind many red blood cells, creating a lump so large as to be visible.



Subtypes hidden

The specificity and thus the hazard of each strain of influenza virus hemagglutinin depends on the particular type he has. They know more than a dozen subtypes of hemagglutinins. Three of these, called H1, H2 and H3 (H is the original English name of hemagglutinin), attacked the man because they are able to recognize specific sugars on the surface of some cells in our section respiratory infection that's why we started there when the flu. Other subtypes such as H5, attack glycoproteins found in the digestive system of birds. Most of these subtypes is not dangerous to humans and not even the threat of bird life and thus constitutes a kind of hidden reservoir of virus. A potential danger, however, may come from the exchange of genes between different strains.

The H5N1 bird flu virus that has come to the front pages during this period, which is decimating the bird population, but is not currently a real danger to humans because they do not have the right to hemagglutinin attack human cells. (The acronym refers to an N1 subtype of a second viral protein surface: neuraminidase that the virus uses to break away from the infected cell and spread the infection). However, there is the possibility that the virus could acquire a hemagglutinin-specific man, and then we can cause real problems. This might, for instance, by pigs. Indeed, the latter are susceptible to both avian viruses to humans that. In cases where a pig was infected simultaneously by both types of virus, they may exchange genes during infection. In this way you could create a new virus with the virulence of avian viruses and more with the ability to attack human cells.

lethal agent

The hemagglutinin shown here has been derived from the virus causing the pandemic that has killed so many people in 1918, the English. The DNA coding for this hemagglutinin was isolated from samples stored and the hemagglutinin was synthesized in the laboratory in accordance with such genetic information. We have obtained two crystal structures, the active form shown here (PDB file 1ruz), and a precursor of the hemagglutinin, not shown (PDB file 1rd8). The protein is attached to the viral membrane by a short filament protein that can not be seen in the crystal structure and that there is schematically represented by the segments beige below.

haemagglutinin in action

The hemagglutinin is a ruthless molecular machine that engages and kills the cells. This process is accomplished in multiple steps.

In the first, the three binding sites on the top of the protein bind to sugars of some cell membrane glycoproteins shown in green in the top left of the figure (PDB file 1hge).

In the second step, the virus enters the cell by endocytosis, ie, the host cell as an endosome, intussusception of the cell membrane, which tries to digest the virus, creating an acid environment. The virus, however, resisted this attack, even the acid environment necessary for him to trigger the mechanism of its counterattack to the cell. Thanks to its acid, hemagglutinin opens and folds up taking a completely different structure. Slices of orange and red are usually tucked inside the protein, but are worn out in acid as shown in the middle of the figure above (PDB file 1htm, 1ibn, 2vir). The red portion is called fusion peptide, has a great affinity for membranes, it is part of the cell membrane and it clips securely to the virus.

In the third step, as shown on the right side of the figure (fike 1qu1 PDB), the portions are wrapped up as orange yellow contract and that makes the protein and forces the two membranes to approach almost to toccasi with each other. Finally, the two membranes fuse and the viral RNA enters the cell beginning the process of infection.

antibodies (mol of the month Sept 2001, Feb 2005, March 2005) are our first line of defense against the influenza virus. The PDB file 1qfu shows how a hemagglutinin antibody attacks the lock so that it can no longer bind to the cell surface.

The structure includes the hemagglutinin, shown in blue and yellow, and three copies of the Fab antibody fragment (the three fragments magenta encase the haemagglutinin).

course viruses develop strategies to escape the attack of the antibodies and thus are born every year new strains still able to infect. One strategy is to change the arrangement of carbohydrates on the hemagglutinin surface. These carbohydrates are shown in green in Fig. If the virus adds a new carbohydrate at the point where the antibody is bound, in the future to prevent quell'anticorpo to bond and have made it ineffective.

Sources:

PDB

What Goes With A Vest

Readings

The increasingly cold and dark days they pushed me holed up in a home with the latest readings looted from the school library. They are the fifth part of Anna Karenina and I just finished reading The 'innocent D'Annunzio, both are wonderful books, full of meaning and able to describe human psychology as nobody believed he could do. Some dialogues have deeply touched me and brought to light old memories, which are tied to the various sensations. Anxiety, doubt, the sense of loss and abandonment, the impression that everything is somehow veiled melancholy are all things that have troubled past-and sometimes still-troubled my mind. But even the love, the joy of seeking the world in the eyes of the beloved , the frenzy that the slightest caress can trigger are all sides of our existence that I had the chance to appreciate. Both texts mostly revolve around love, it is troubled, hurting and adulterer, or that it is pure, high and true, being able to analyze it in depth but does not deprive him of his romantic mystery. I was really enchanted by the evocative power of those words and again I wondered how it was possible that two strangers were able to describe with minute accuracy the complexity of my joys and my troubles. This makes me reflect on the fact that, for all unite us, has always been and always will be the fact that be swept away at any time by ' inevitability of feelings, however understandable in their entirety only to a select few, with a higher sensitivity, and I strongly believe that D'Annunzio Tolstoy belong to this group of elected officials.

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Two months

I wonder how my life would be now if you had not returned to join. If it were not for your lips to my warm up after a walk through the streets of this obvious gray province. If it were not for your voice and your face to be recognized among the multitude daily. Your presence in my heart is a protection against all the hatred, resentment, superficiality violently from all that rain and will certainly end up with hurt me if I tried all this boundless love . If I had not returned to them so sweet and determined to wind I finished my thoughts with the old veil of mistrust in which I found under the illusion of strength. If I had never looked deep in your beautiful eyes I would have resigned blacks to human cruelty, some could not hope for anything more than the usual phrases of circumstance. But you're new here, you're back to being the center of my every action, the root cause of all my joy. If there were more people in the world with your own sensibilities would no doubt much less vulgarity and much less perfidy to poison the present day. I love you with all the overwhelming intensity that my feelings can get to try.

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RNA interference.

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( I've edited the post on RNA interference, making it much more complete).

L '

RNA interference (RNA interference) was discovered for the first time in a nematode worm (Caenorhabditis elegans



). It was observed that the double-stranded RNA (dsRNA
, double stranded RNA
) caused gene silencing in a sequence-specific. Researchers had long thought that the RNA would be a perfect tool for the control of gene expression, since the right sequence of RNA should bind DNA and interfere with its transcription. While studying the efficiency of antisense RNA as a suppressor of gene expression, it was found that dsRNA was more efficient to turn off the transcription of a gene.

In our cells the presence of double-stranded RNA can be a big problem. Although cells are present in the transfer RNA
and ribosomes, which contain some sharp edges hairpin and then double helix, most of our RNA, and especially the messenger RNA is a single chain. Many viruses, however, form long stretches of double-stranded RNA as their genome doubling. If our cells are double-stranded RNA, interpret it as having a viral infection and produce a response that often leads to death of the entire cell. The plants and animals, however, has other defenses targeted directly attack viral RNA, called RNA interference

.

Since its discovery it has been observed that the mechanism of RNA interference was also present in plant cells, in which is a way to degrade the viral RNA. its function as a result was also observed in Drosophila and mammals. At present it is believed that RNAi is a natural regulatory mechanism that controls gene expression. It could also be a protection mechanism against harmful gene products oncogenes that summarize too much.

produce interference

as shown at the top of RNA interference begins when you submit a long chain of double-stranded RNA such as that produced by virus replication. An enzyme class is RNase III known as Dicer (which fragments), shown at the top right in blue (PDB file 2ffl ), binds to the dsRNA sequence of cutting the chain small fragments called short interfering RNA (

siRNA), one of which is shown in the upper left (PDB file

2f8s

). The siRNA is about 21 base pairs long, but the two chains are cut in an asymmetrical way: 19 nucleotides are perfectly paired as two nucleotides protruding from each of the two 3 'end. These features readily recognized by the siRNA. It seems that a key role nell'enzima Dicer, is played by special arrangement of four manganese ions, highlighted in magenta in the facility. It is thought that these are just to make the cut in the chain of asymmetric double-stranded RNA, thus creating the projections.

The fragment obtained by the catalyzed by the protein Dicer is associated with an enzyme complex called RISC

(

RNA-interference silencing complex, the RNAi silencing complex ). double-stranded RNA is opened, probably by a helicase, only the antisense RNA strand remains bound to RISC, while the sense strand is degraded. The RISC binds to a complementary sequence of a fragment of mRNA degrading. Why this happens is still under investigation. Probably a

endogenous RNA polymerase somehow manages to feel that a particular messenger RNA is produced in excess through the different reactions we have described to trigger the process of destruction. After all if we think about it is a logic that could also be applied against the virus. In recent years, many industries have arisen that have built kits for RNAi and dsRNA for use in laboratory inactivate genes. In fact, once the known gene sequence of our interest in the double-stranded RNA can be used to produce the siRNA to turn off the gene using RNAi these researchers were able for example to map thousands of genes organism

C .

elegans.

Protein Argonaut siRNA molecules produced by the enzyme Dicer, are also collected by proteins known as the Argonaut and used to destroy any other RNA that are close by. The Argonaut protein, shown here at the bottom (PDB file 1u04) alloy upon himself one of the two chains of siRNA and look for a messenger RNA that is equip with it. If found, it hydrolyzes, that destroys it. In this way, the cell removes all traces of messenger RNA that corresponds to the sequence of the double helix of RNA attached to the top by the enzyme Dicer. Trivia: Argonaut protein was discovered for the first time in a plant mutant that had a spiral shape similar to that of the Nautilus shell, the British call a cephalopod Argonauta. many RNA ...

In the years since the discovery of RNA interference, researchers have found that this process is much more common than expected at the beginning and that small fragments of RNA plays many functional roles. A similar class of molecules called microRNA, is created in the core from the normal RNA of the cell. Even these microRNAs are created by Dicer enzyme and are used to modulate the activity of our normal messenger RNA. Looking for a messenger RNA with a complementary sequence, will bind, and then they stop functioning. MicroRNAs are coupled with complementary sequences of DNA, thus changing the properties of the chromosomes by changing the level of methylation or histone binding.

In the search ...

Scientists have learned to use the technique of RNA interference to destroy specific RNA sequences in animal and plant cells. Exploiting this process, the researchers were able to synthesize artificial interfering RNA sequences which, inserted into the cell, RNA can destroy whatever you want to disable. As mentioned before percmette this technique to study the genes and what may be their function. For example, RNAi is destroyed most of the messenger RNA that produces the gene using RNA interference, which can bind to specific mRNA, thus almost completely stops the production of the protein that is encoded by the gene and observed the consequences. Some researchers are trying to use these small molecules RNA to combat diseases, such as turning off certain genes linked to cancer.

Strategies virus.

viruses, however, have many tricks up their sleeves and rarely left without doing anything when they were attacked. Viruses have developed different strategies to respond to RNA interference. The protein shown here (PDB file

1r9f ) is a protein produced by the suppressor virus tomato bushy rickets.

binds to siRNA and prevents the normal function to destroy the viral messenger RNA. Notice how the protein (in blue) to act as a gauge, overlapping at both ends of the siRNA (orange and red). In this way detects and blocks only small fragments of RNA that have exactly the length of an siRNA.

A look at the structure ...

siRNA molecules produced by the enzyme Dicer are easy to recognize: they all have the same length of 21 base pairs and have an unusual tail of two nucleotides protruding from each end 3 '. The structure shown above in blue (file 1si3 PDB) is the PAZ domain used by many proteins to recognize the two ends of the siRNA. The protein is linked to a short stretch of siRNA represented by small colored balls. Note, in the upper left, as the two bases protruding bind within a small pocket of the protein, while the base terminal of the shorter chain, right, rests just below a ledge of the protein.

Here is a movie of the mechanism of RNA interference directly from the site of still

(

RNA interference mechanism

Sources:

PDB (Protein Data Bank

);

Nature

.

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♥ The devil is in the details

A lot of people are surprised by my good memory, especially for dates, birthdays or other significant events, I do not seem nothing special even though I recognize that you have a particular talent for to recall the details . Facial expression, a casual hand gesture, a word seemingly trivial things are all that, when inserted in a relevant context for me, going to store in memory, intended to stay in indefinitely. Not always have positive consequences because in addition to having saved so many times that I have filled with joy , lots of unique moments and sweet are also able to remember with painful accuracy the ugliest periods, those full of confusion and loneliness . Sometimes it happens that my subconscious makes me sick to relive those memories in the form of distressing nightmares and strange, like those of a few nights ago, or those of a few weeks before. What troubles me about these dreams is not so much the memory itself but rather the fact they are reliving a situation where I was weak and afraid, so no full stops or certainties. Despite this summer have changed for the better aspects of my life some things just can not forget, I chose to forgive, to move forward without opening old wounds but - unfortunately - I can not choose what to remove from my head.

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small RNAs that induce tumor cells to self-destruct

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