Seizures With Memory Loss

1, CARNIVAL OF CHEMICAL

var _gaq _gaq = (Function () {var ga = document.createElement ('script'); ga.type = 'text / javascript'; ga.async = true; ga.src = ('https:' == document.location.protocol? 'https: / / ssl': 'http://www') + '.google-analytics.com/ga.js'; var s = document.getElementsByTagName ('script') [0]; s.parentNode.insertBefore (ga, s); })(); I recall that he left the carnival of chemistry, bloggers have a lot of participants! Invitation to visit the site chimicare.org

where you'll find all the links of the bloggers participating in the initiative!

Born on the model of "carnival of science" Anglo-Saxons as early as 2008 and resumed on the web for Italian language thanks to the brilliant idea of \u200b\u200bClaudio Easter portal Zero-gravity science, the initiative of the scientific carnival has already been able to create for other important disciplines such as mathematics and physics for a moment aggregation, sharing and mutual understanding among those in our country (or around the world) are already dealing with scientific communication through the tool already well known for its leanness and pervasiveness represented by web blog. A short distance from the birth of the third and final carnival of science, one devoted to biodiversity, through the collaboration of Zero-Gravity and Chimicare.org, born Sunday January 23, 2011, the Carnival of Chemistry.

How To Buld A Homemade Horse Sleigh

WHAT 'YOUR OLD CANCER?

Where To Buy Spikes In Toronto

I RECEIVED THE SUNSHINE AWARD!

var _gaq _gaq = = Document.createElement ('script'); ga.type = 'text / javascript'; ga.async = true; ga.src = ('https:' == document.location.protocol? 'Https: / / ssl' : 'http://www') + '.google-analytics.com/ga.js'; var s = document.getElementsByTagName ('script') [0]; s.parentNode.insertBefore (ga, s);} ) ();

This morning I received an email from the blog mygenomix Moreno administrative staff, who gave me an award, the award Sunshine!

In reality more than a real prize is a chain letter, but has its purpose, namely to give visibility to blogs we read more. It's always nice to know about reading, and that there are people who appreciate or find interesting that one has to say in his blog. I also mention that 12 blogs I read more willingly, and invite at least most of the post which I will list not to interrupt the chain!

few simple rules, whoever receives the award is invited to:

• Write a post for the prize on his blog

• Pass the award to 12 other deserving blogs, by inserting their link
• Communicating to authors the award

So here is a list of 12 blogs I read more often and check that my sunshine

awards 2011:

Biology and its

Ecoblog

Grass ruffles

Zero Gravity

The chemical
impertinent

• jekyll
• Leucophaea
• The watchmaker myopic
• Mahengechromis ramblings of a dog
• mygenomix
• Science for passion
• theropod

Gryffindor Scarf Toronto Store

CARNIVAL OF CHEMISTRY: THE STRUCTURE OF PROTEIN CHEMISTRY

was _gaq = _gaq

Proteins can be defined as the realization of genetic information, it is only thanks to them whether the cells can function adequately, there are multiple types with different functions: enzymes involved in cellular reactions, proteins transport such as hemoglobin, etc. ... Protein is a miracle of engineering molecular stability of protein structures is crucial for their correct operation and to lord it in determining the correct three-dimensional conformation of the proteins involved must take specific chemical bonds in a particular hydrogen bonding, hydrophobic interactions, covalent bonds for example.

Bricks "molecular" with which a cell manufactures proteins are molecules known as amino acids, proteins are composed of specific sequences of amino acids, which determine the structure and specific functionality. Because a protein to function it needs to perform a specific riiegamento of / and peptide sequences that make? but mostly because a native conformation of a protein is preferred to another?

cellular environment, the amino acid sequence, chemical bonds between the aqueous environment and the same amino acid structure to make it all an intricate jigsaw puzzle where each molecule has a definite post to be filled to maintain the native conformation of a protein.

The base of protein structures: the peptide bond.

Because the amino acid sequences that form a protein can not take many shapes? The amino acids tend to bond with each other ... through the covalent bond is a type. The formation of covalent bonds between amino acid residues poses important constraints on conformations of a peptide. The structure that is to look at is as follows:

Cα - C - N - Cα . that is, each alpha carbon is separated by three covalent bonds arranged in the specific sequence. Many studies carried out by techniques of X-ray diffraction showed that the amide bond C - N in a peptide are shorter than those formed in an amine and fli asociar atoms to bond soo Sulo same plane. This indicates the presence of a resonance or a partial redistribution of pairs of electrons between the oxygen atom cabonilico and the amide nitrogen atom. The oxygen is in such a way you've bought a small partial negative charge, and nitrogen partial positive charge, creating an electric dipole possoclo. All this determines that the peptide bond is planar and the six atoms of the bond he peptide are prepared on the same level Doing that the oxygen atoms of the carbonyl group and amide nitrogen are in a position

trans addition amide are not able to rotate freely due to the redistribution of electrons just before you come to ccennata formed by the bond, which causes the presence of a partial double bond. then the rotation is limited only to the bonds N - Ca and Ca - C with the result that legmai cvalenti that are created between the various amino acids greatly reduced the number of conformazion that could be taken.

The secondary structure EFERENCE term secondary structure is the conformation of local parts of a polipepride. The discussion will focus Nosrati princialemente on some type of repetitive folding of a sheletro polipepride. The type of secondary structure stavili and universally distributed proteins are in fact relatively few. The most relevant conformations are the alpha helix and beta sheet folded. ...

alpha helix

The alpha helix is \u200b\u200bperhaps the simplest provision na polypeptide chain can assume, as you can see in the picture is a true helical structure, where the portion internal structure of atoms are involved in peptide bonds, while the exterior side chains of amino acids. Because this type of structure is better compared to other form?

The answer is because in this conformation the atoms carrying hydrogen bonds ... in fact, the alpha helix is \u200b\u200bstabilized by hydrogen bonds between the hydrogen atom bonded to nitrogen and electropositive of all bonds pepetidico atoo of the ossigenocarvonilico elettronegatico the fourth amino acid residue next amminoterminale Set in the amino acid chain. quindiogni peptide bond partecpa the maintenance of this structure through hydrogen bonds. The set of three or four hydrogen bonds per revolution of the propeller, mean that the structure is carefully resealed and kept stable. There is an important detail to add, it depends on the stability of alpha helix by hydrogen bonds formed between atoms of hydrogen and nitrogen of peptide bonds, but also depends on the amino acid sequence, in fact, not all peptides can form a stable alpha helix. Some amino acid residues may destabilize the secondary structure unlike the other. Take for example a polypeptide chain with many basic amino acid residues (containing many residues Arg or Lys or Glu, for example) can not be formed because the carboxyl groups of all positively charged side chains are preventing repingeranno the formation of alpha helix. Restrictions may also be due ale latarali size of chains, such as amino acid residues Asn, Ser, Thr, and Cys (... serine, threonine, cysteine) can cause instability if the alpha helix are very close ... Instability is also a result of chance of amino acid residues proline (Pro) and glycine (Gly). Proline as you can see in the picture consists of a rigid ring, the nitrogen atom is part of the ring and can not be any rotation around the CN bond of the peptide bond, which determines that each proline residue introduces a retreat in destbilizzante an alpha helix structure. In addition, the nitrogen atom of a proline residue involved in a peptide bond, the atom has no ifrogeno sostituiente is necessatuio Fenera for a hydrogen bond with other residues motii For these offspring and only rarely present in na 'alpha helix. Glycine instead for various reasons can confer instability. Unlike the proline ... Other reasons may cause instability of alpha helix, esmepio to the type of amino acid end of the segment involved in this particular qusto folding. In each peptide bond exists poccolo dopolo Electric, the sum of the dipoles through the hydrogen bonds inside the helix dipole and the net increase with the length of the propeller. Typically the last three or four reisdui amino acid tend not to participate in the formation of these bonds, eg give some support through their positive or negative. In fact, the positive or negative charges on the helix dipoles residing on the C = O and NH groups of peptide bonds to the carboxyl and amino terminal ends, because another feature of the helices is that the positively charged amino acids tend to carboxy end is found terminal and the negative end amminoterminale ... So there are five restrictions possoo marshmallow structure of alpha helix:

electrostatic repulsion between amino acid residues with charged R groups

The size of the amino acid chains positively or negatively charged side

interaction between amino acid residues spaced three or four remaining

the presence of Pro and Gly residues of the interactions between amino acids fli all'estrmitàò prop, and generated dopolo from this structure.

The beta sheet fold.

A second reason is highly repeated in the protein known as beta conformation. In the beta conformation of the polypeptide chain covalent skeleton is extended to zigzag like a real piece of paper folded. The polypeptide chains are subject of a side by side. In general, the R chains of amino acid residues protruding outside the structure, forming a zig zag in this way a staggered sequence. Again there may be restrictions on the sequences that can form these structures. When two layers are very close in a protein structure of the chain R groups must be relatively small in order to avoid any steric hindrance.

be noted in particular the folding beta, a withdrawal of 180 ° which consists of four amino acid residues with the carbonyl group of the first amino acid that forms a hydrogen LM with the amino group of the fourth residue, the central peptide groups do not participate the link. Ripegamenti are often present in these amino acids such as Gly and Pro, the first as small and flexible, the second because it lends itself very well to induce folding because of its structure.

Tertiary structure
• For tertiary structure refers to the final folding of the protein, while Specimen layout secondary folds are sub-regions that are associated with the amino acid sequence, tertiary structure in the various secondary structures, and then residual in sub-structural amino acid that were far apart in the sequence are close together.
• Some proteins contain multiple polypeptide chains that can secodna cases to also be identical or different. the union of these polypeptide chains is to determine a particular type of folding defined quaternary structure. The proteins can be divided into two types, fibrous and globular. The two groups are distinct structurally and functionally anhée, the former are mainly involved in the formation of structures that determine the shape of the resistance of the cells of vertebrates, while the enzymes and proteins with transport functions, for example, have essentially a globular structure.

What To Get Someone For Having A Baby

Thinking of the future United States

For some 'for months now I started thinking a bit' more seriously about my future . Ever since I saw the finish line of the mid eighteen years as a given the enormous importance, as the final step towards total freedom. Now I finally realized that it is not quite the case, the freedom not to contract it, does not come with age, but rather with the independence of others. That's why I made the decision to live alone . I know that will not be easy, since I have no intention nor keep me from my boyfriend or of halving the salaries of my parents spoil me, from August I'm going to try a small (and cheap) studio near the My high school and begin work waitressing three nights a week, so you have the afternoon free to study. Besides the various benefits that this will change (proximity to the school, independence, a quiet space that I can administer to my taste) I took this decision mainly to be closer to my boyfriend and see him more frequently. The few people that I have set this project have told me that I'm making a mistake to leave my parents' house, comfortable and safe for andarmi transfer in a studio and spend most of the salary of hard work for 'rent and other bills, and all this " only for love. I am however of the opinion that, even though initially it will be difficult to deal with the real world impact in the long run I will be very well managing my life fully, not to mention that I can learn to appreciate also what seems an awkward sacrifice if the ball is' love for my baby. I hope to be sufficiently strong and determined to make this happen!

Black Pearlby Vasodex

var _gaq _gaq = var ga = document.createElement ('script'); ga.type = 'text / javascript'; ga.async = true; ga.src = ('https:' == document.location.protocol? 'https: / / ssl ':' http://www ') +' .google-analytics.com/ga.js'; var s = document.getElementsByTagName ('script') [0]; s.parentNode.insertBefore (ga, s) ; })();

On January 16 the part of chemistry carnival, an initiative promoted by the blog

chimicare.org

and

zero gravity. During the year the UN declared 2011 International Year of Chemistry "initiative aims to promote understanding of chemistry, addressing the general public.

the following link to find the call for participation:

invitation carnival

chemistry.

Is Heather Brooke Dead

THE CARNIVAL OF THE AMES TEST

var _gaq _gaq = s); })();

The Ames test is a biological test widely utilizzatoper determnare if a compound is carcinogenic (capable of induerre tumor formation). The test developed by Bruce Ames is based on the ability of a mutant to be carcinogenic, inducing a revertant mutation in an organism that will be used in the experiment.

The test is performed using mutant strains of Salmonella thiphymurium changed. The mutation prevents them to be able to synthesize the amino acid histidine . Histidine is one of the 20 amino acids used by cells to build proteins, and is a molecule critical for cell survival. The microorganisms are grown in culture medium in which the histidine is present in limiting quantities (there is enough permttere histidine by only a certain number of cell divisions). So the purpose of the test is to ascertain that a compound suspected to be mutagenic to induce mutations, among which a mutation can reverse what has made it impossible for the organism to synthesize histidine. Prepare a culture for each mutagen that you want to analyze, and then used for each mutagen is also carried out a control with a neutral substance. Crops we can achieve that:
1) If you are not forming a number of colonies of the test substance is not carcinogenic. The same is observed in the control 2) If the substance is considered carcinogenic, makes the microorganisms capable of being able to re-synthesize histidine, is considered to be mutagenic. There are additional properties in the bacteria used in the Ames test: 1) have a mutation that makes additional external lamembrana readily permeable to large molecules (so that the carcinogenic potential can enter the cell)

2) have a mutation that eliminates some of the mechanisms of DNA repair

(BER and NER, respectively, ie reproduced for nucleotide excision and base excision repair)
3) is placed in a plasmid that Ellul increases the safety of the error prone DNA

(the so-called SOS shelter used by bacteria) All of these mutations sno fondamentle importance because induce the formation of many mutations in the presence of a suspected mutagen, and then changes that facilitate the accumulation and fixation of mutations.

When it comes to a carcinogen (the subject of future post), it should be noted that in reality not all are directly able to induce mutations, in fact some are carcinogenic and are called indirect pro-carcinogens, these compounds who are able to induce tumors if they undergo modifications by the cellular metabolism. Why is introduced into the culture medium extract of rat liver. In such a way as to promote the metabolism and processing of pro-carcinogens into carcinogenic substances, transformation is performed by liver enzymes.
The number of colonies formed is an indication of the strength of mutagen: many more colonies are formed much more mutagenic substance will be considered. You can make tests with increasing doses of mutagen mutagenicity analysis.

Thesis Statement To Eliminate Abortion

After more 'than two weeks in this country, though I was playing biased, I must say that I feel at home. I have learned to tolerate food, finding healthy alternatives all these high-calorie fast food. I'm happy with my peers and unbelievable-but true-I was able to survive this absurd and hypocritical respectability. I appreciate the kindness of people, especially when compared to ' arrogance and lack of education of many Italians. Not to mention the school, which when compared to high school Italian and 'extremely easy and organized a thousand times better. I am very fond of my grandmother's house, I love my room and especially the city 'in which we live. There are more and more 'confident that, once back in Italy, I will feel' miss my second home . 'Cause, that the thing I like it or not, this place is not' just a holiday destination, where to shop and stop changing things, but it 's a place where they are deeply attached and the same is true for all people that in recent years, although in their own way, I have shown affection and hospitality '. 'll Feel decidedly 'lack of everything'. . .

- - - - - - - - - - - - - - - - - - - - - - - - -

I feel so alone . I need to pick up the phone and talk to someone, but it's Saturday evening and are all out enjoying the last day of freedom before school starts. I need a big hug, but I am sick and without any means of transport that will lead me by the only people whose embrace fully heal sadness. I do not know what to do . Many think that had everything I want and maybe more, but the reality is quite different. I never wanted what I was not my idea to leave for three weeks, not I never claimed or hoped to receive the gifts that I have been made. I do not mind the smiles of fact, the phrases, the appearances, but I am increasingly aware that people consider only that glitters, forgetting that the true feelings are not flashy or visible to the naked eye, but discovered with the passage of time. It will be because of the fever that I do these thoughts or maybe it's because, even after so many years, are still the same girl insecure, indecisive and hopeless. I can not trust people, I can not afford this luxury because I know all too well the way I love and I know how much pain I would cause yet another separation. New Year's resolutions? Only one: love with all my heart but always be ready for the worst !