User:AdvInorgChemMan/sandbox

adding text as a test

maybe a couple more tests

wikipedia.

Week 3 tasks: info for Ammonium Vanadate

Properties of Ammonium Vanadate

-NH₄VO₃

-116.98 g/mol

-

AdvInorgChemMan/sandbox

Names
IUPAC name Ammonium Vanadate
Identifiers
Properties
Chemical formula	NH4VO3
Molar mass	116.98
Appearance	Powder or Crystals
Density	2.33 g/cm^3
Melting point	200 C
Boiling point	N/A
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). Infobox references

Ammonium Vanadate

Ammonium Vanadate

Ammonium Sulfate

Aluminium Chloride

Organic solar cells

Self destructing Plastic

Practice Uploading a PDB Structure Image

PDB

Critique of Carbonic Anhydrase Mechanism Figure

Bilal added the first paragraph to the reaction and 2 images, including the mechanism in question

The arrow mechanisms are not text book quality and is not sufficiently detailed. It does not look professionally drawn as the arrows used are of different sizes and poorly done in chemdraw. The bond angles/bonds in general appear to be correct but it is missing a title.

Practising tables and formulas

Ammonium Chloride (ClH₄N)

Molecular Weight	53.491 g/mol
Density	1.53 g/cm3
Melting Point	338°C
Boiling Point	520°C

A_a + B_b --> C_c + D_d

$\log _{10}+\exp _{7}$ - 3⁹

${dy \over dx}+{da \over dc}-\left({\frac {1}{5}}\right)$

Practice Using History Pages, Talk pages, Article ratings and Watchlists

Iron-sulfur cluster

The main purpose of the edits by smokefoot were to reduce the amount of information on the wiki page since it was filled with too much and unnecessary information. The negative numbers are the text that they removed because they deemed it unnecessary and stated that "Wikipedia is not a school essay". I believe the edits were necessary since there was so much information on the page and removing it didn't impact the page negatively, in fact, I believe it benefited the page more

talk

Hello,

I hoping to contribute, my knowledge to this article by discussing the strength, covalency and electron transfer effects. Ninja Recs (talk) 01:00, 12 October 2018 (UTC)

You are writing at a level that indicates that your teacher is needed. Please ask your teacher to read some Wikipedia articles first. --Smokefoot (talk) 01:20, 5 December 2018 (UTC)

Carbonic anhydrase

Smokefoot appears to be trying to reduce the clutter and any repeating points to make the article clearer for the viewers, the negative number indicates that he is removing words and lines from the article. Smokefoot's makes a good improvement on the article because they made the article easier to read and understand by changing a few things.

The new paragraph that bilal edited did provide more information and was easy to read so I believe it helped the article. The previous article is lacking information in the introduction.

The article edited by bilal is still in the article but is polished and references were added to make it a more complete paragraph with a slightly better way of giving the information.

There seems to be a decent amount of information discussed in the talk tab of the article, since it is only rated C it is expected to have a bit of information exchange. There has been over 250 edits since 2004 so I would have expected a bit more in the talk tab.

Ceruloplasmin

The multicopper active site of CP contains a trinuclear copper center with a type I (T1) mononuclear copper ~ 12-13 Å away (see figure 2).  The trinuclear center consists of two type III (T3) coppers and one type II (T2) copper ion.  The two T3 copper ions are bridged by a hydroxide ligand while another hydroxide ligand links the T2 copper ion to the protein.  The trinuclear center is bridged by two histidine (His1020, His1022) residues and one Cys(1021) residue.  The substrate binds near the T1 center and is oxidized by the T1 Cu²⁺ ion forming the reduced Cu⁺ oxidation state.  The reduced T1 Cu⁺ then transfers the electron through the one Cys and two His bridging residues to the trinuclear copper center.  After four electrons have been transferred from the substrates to the copper centers, an O₂ binds at the trinuclear center and undergoes a four-electron reduction to form two molecules of water.        

Figure 2: Close-up view of the CP active site consisting of the T1 copper center (left) and trinuclear copper center (right) showing the coordinating side chains. PDB code: 1KCW. Atom colors: Cu = grey ; O = red ; N = blue ; S = yellow.

Despite extensive research, much is still unknown about the exact functions of CP, most of the functions are attributed to CP focus on the presence of the Cu centers. These include copper transport to deliver the Cu to extrahepatic tissues, amine oxidase activity that controls the level of biogenic amines in intestinal fluids and plasma, removal of oxygen and other free radicals from plasma, and the export of iron from cells for transport through transferrin.

Mutations have been known to disrupt the binding of copper to CP and will disrupt iron metabolism and cause an iron overload.

Ceruloplasmin is a relatively large enzyme (~10nm); the larger size prevents the bound copper from being lost in a person’s urine during transport.

Clinical significance:

Ceruloplasmin can be measured by means of a blood test; this can be done using immunoassays . The sample is spun and separated; it is stored around 4°C Celsius for three days. This test is to determine if there are signs of Wilson disease. Another test that can be done is a urine copper level test; this has been found to be less accurate than the blood test. A liver tissue test can be done as well.

AdvInorgChemMan/sandbox

Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). Infobox references