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EBooks by Jomegat

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Posted: December 31st, 2011, 11:32pm CET by Jomegat

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Your [[Special:Contributions/KANNEBEN000|recent edits]] are considered unconstructive by fellow contributors. Please read [[WB:WIW|What is Wikibooks?]] for a description of what we allow. You can ask questions or ask for help in the [[WB:HELP|Assistance Reading Room]]. Please use the [[Wikibooks:Sandbox|sandbox]] for experimenting with the wiki software in the future. Thanks. --[[User:Jomegat|Jomegat]] ([[User talk:Jomegat|discuss]] • [[Special:Contributions/Jomegat|contribs]]) 22:32, 31 December 2011 (UTC)}}

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Posted: January 2nd, 2011, 6:40am CET by Jomegat

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Block notice

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Posted: January 2nd, 2011, 6:39am CET by Jomegat

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blocked [[69.178.194.88 (talk)]] with an expiry time of 3 months (anonymous users only, account creation disabled) vandalism


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Posted: December 23rd, 2010, 6:09am CET by Jomegat

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unexplained removal of text

← Older revision Revision as of 05:09, 23 December 2010
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Now add in a different class, the people from the new class would have their own tertiary structure, these new people will then come in and react with the original class to form <u>quaternary structures</u>. Now add in a different class, the people from the new class would have their own tertiary structure, these new people will then come in and react with the original class to form <u>quaternary structures</u>.
  +
  + ===Human attempt to manipulate protein assemblies (Quaternary Structures)===
  + Controlling the quaternary structures is currently catching more and more interest in academics. There are many advantages in manipulating protein assemblies. Firstly, people are able to grow/synthesize enzymes that are beneficial to human. Yet, to get these enzymes to work is the hard part. For example, nitrogenase, the enzyme that can fix nitrogen gas to yield ammonia, can only work under aerobic environment and coupled with ATP as energy source. In addition, researchers have revealed that nitrogenase is compose of two proteins, one for ATP coupling&electron source and the other is the reactive center for nitrogen fixation. The two protein assemble to work as a whole. Recently, scientists remove the ATP coupling protein and replace it with a Ruthenium complex. It turned out that Ruthenium complex can provide electrons with light exposure. Now scientists don't have to deal with the complicate chemistry of coupling ATP, but just shine lights on engineered nitrogenase to get it work! Secondly, protein assemblies can have a lot of clinical/material applications. Ferritin is a family of high-order protein assembly family, usually 12mers or 24mers. Previous researches showed it can absorb large amount of Fe ion. Many researchers are working to control the association and disassociation of Ferritins, seeking for solutions of drug delivery, gas storage, metal harvest and etc. Many approaches have been developed to control protein assembling. Following are some of them.
  +
  + 1. Transition metal-directed. Metal centers in protein are important, not only because they are reactive centers, but also they help stabilize the shape of protein by coordination. Many amino acids are ligands by themselves. Cysteine, Histidine, lysine are the common ones. Plus, researchers can engineer inorganic ligands onto proteins by cysteine substitution. Thus, introducing inorganic ligands much broaden the horizon of protein assemblies.
  + [[Image:phen.jpg|thumb|the structure of Phenanthroline (inorganic ligand).]]
  + [[Image:terpy.jpg|thumb|the structure of Terpyridine (inorganic ligand).]]
  + Metal-ligand bonding has several properties. Most obviously, it is a strong interaction. It is stronger than hydrogen bond and weaker than colvant bond. Therefore metal-ligand bond is strong yet not so strong that it is still reversible. Spatially speaking, metals have its coordination orientation, mostly, octahedral and tetrahedral. This property provides human great convenience in arranging proteins spatially.
  + [[Image:bisterpy.jpg|thumb|shown is the cartoon model of a dimer of two terpyridine-labeled proteins.]]
  +
  + [[Image:triphen.jpg|thumb|shown is the cartoon model of a trimer of three phenanthroline-labeled proteins.]]
  +
  + 2. Hydrophobic interaction. In aqueous environment, amino acid with hydrophobic side chains tend to aggregate together to minimize the exposure to water. Researchers utilize this character and engineer certain matching pair of non-polar amino acids onto proteins to obtain protein oligomers in water solution.
  +
  + 3. Salt bridges. It is well known that amino acids have different pI's. So at certain pH, some amino acids are negatively charged, some are positively charged. If an area on a protein is occupied by mostly negatively charged amino acid and another area is occupied by positively charged amino acids, proteins can aggregate by electrostatic attraction. However, this technique is usually not so selective.
  +
  + More technique to direct protein assemblies are being investigated, such as coiled-coil. Human's ability to control quaternary structures is promising.
  +
  + {{BookCat}}

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Posted: December 21st, 2010, 2:15am CET by Jomegat

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Obscured Page Title

← Older revision Revision as of 01:15, 21 December 2010
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Hi, It seems to have been fixed. Thanks, [[User:Armchair|Armchair]] ([[User talk:Armchair|talk]]) 21:42, 20 December 2010 (UTC) Hi, It seems to have been fixed. Thanks, [[User:Armchair|Armchair]] ([[User talk:Armchair|talk]]) 21:42, 20 December 2010 (UTC)
  + :It's obscured now in Firefox 3.0.15 (I should upgrade some day). --[[User:Jomegat|Jomegat]] ([[User talk:Jomegat|talk]]) 01:15, 21 December 2010 (UTC)

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Posted: December 15th, 2010, 2:49am CET by Jomegat

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Please be constructive

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{{tmbox|type=delete|text='''Please help <u>''improve''</u> Wikibooks'''.

Your [[Special:Contributions/71.48.190.81|recent edits]] are considered unconstructive by fellow contributors. Please read [[WB:WIW|What is Wikibooks?]] for a description of what we allow. You can ask questions or ask for help in the [[WB:HELP|Assistance Reading Room]]. Please use the [[Wikibooks:Sandbox|sandbox]] for experimenting with the wiki software in the future. Thanks. --[[User:Jomegat|Jomegat]] ([[User talk:Jomegat|talk]]) 01:49, 15 December 2010 (UTC)}}

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