Proteopedia - User contributions [en]

User:Ying Zhao/Sandbox

2012-05-04T20:37:48Z

Ying Zhao:

<ref name="Structural">PMID:15713683 </ref>

It is possible that OspB performs an autoproteolysis. There is a set of three residues found on OspB that resembles the catalytic triad of Serine_Proteases. This "constellation" consists of Thr-166, Arg-162, and Glu-184, which is similar to the catalytic triad residues of the serine protease trypsin, which are Ser-195, His-57, Asp-102 <ref> PMID:12475199</ref>.

Threonine and Glutamic acid are found in other catalytic triads of the serine hydrolase family, but argenine seems unlikely to replace histidine as a base because of its higher pKa. There have been studies that have shown that Argenine is essential for other enzymatic functions, such as in the Ser-Arg-Asp triad in cytosolic phospholipase A2 and as a catalytic base in Sortase A. Asn-164 forms an H-bond with Thr-166 and may rearrange to form a putative oxyanion hole with Thr-166 and another unidentified atom if active in the catalysis <ref name="Structural"/>.

It was recently discovered that all antibodies contained Fab portions that catalyzed a reaction between singlet oxygen and water, yielding hydrogen peroxide, ozone, water and hydroxide radicals. Hydrogen peroxide is a toxic oxidative species and might be the product of an ancient mechanism to protect against infection. UV absorption increases the rate for this reaction. B. burgdorferi is especially vulnerable to oxidative damage because its ecological niche is in areas with limited oxygen and its genome does not encode a catalase. This oxidative mechanism might explain why some mABs are bactericidal without the use of complement. <ref name="Structural"/>.

==References==
<references />

User:Ying Zhao/Sandbox

2012-05-04T20:37:22Z

Ying Zhao:

<ref name="Structural"/>PMID:15713683 </ref>

It is possible that OspB performs an autoproteolysis. There is a set of three residues found on OspB that resembles the catalytic triad of Serine_Proteases. This "constellation" consists of Thr-166, Arg-162, and Glu-184, which is similar to the catalytic triad residues of the serine protease trypsin, which are Ser-195, His-57, Asp-102 <ref> PMID:12475199</ref>.

Threonine and Glutamic acid are found in other catalytic triads of the serine hydrolase family, but argenine seems unlikely to replace histidine as a base because of its higher pKa. There have been studies that have shown that Argenine is essential for other enzymatic functions, such as in the Ser-Arg-Asp triad in cytosolic phospholipase A2 and as a catalytic base in Sortase A. Asn-164 forms an H-bond with Thr-166 and may rearrange to form a putative oxyanion hole with Thr-166 and another unidentified atom if active in the catalysis <ref name="Structural"/>.

It was recently discovered that all antibodies contained Fab portions that catalyzed a reaction between singlet oxygen and water, yielding hydrogen peroxide, ozone, water and hydroxide radicals. Hydrogen peroxide is a toxic oxidative species and might be the product of an ancient mechanism to protect against infection. UV absorption increases the rate for this reaction. B. burgdorferi is especially vulnerable to oxidative damage because its ecological niche is in areas with limited oxygen and its genome does not encode a catalase. This oxidative mechanism might explain why some mABs are bactericidal without the use of complement. <ref name="Structural"/>.

==References==
<references />

User:Ying Zhao/Sandbox

2012-05-04T20:35:37Z

Ying Zhao:

It is possible that OspB performs an autoproteolysis. There is a set of three residues found on OspB that resembles the catalytic triad of Serine_Proteases. This "constellation" consists of Thr-166, Arg-162, and Glu-184, which is similar to the catalytic triad residues of the serine protease trypsin, which are Ser-195, His-57, Asp-102 <ref> PMID:12475199</ref>.

Threonine and Glutamic acid are found in other catalytic triads of the serine hydrolase family, but argenine seems unlikely to replace histidine as a base because of its higher pKa. There have been studies that have shown that Argenine is essential for other enzymatic functions, such as in the Ser-Arg-Asp triad in cytosolic phospholipase A2 and as a catalytic base in Sortase A. Asn-164 forms an H-bond with Thr-166 and may rearrange to form a putative oxyanion hole with Thr-166 and another unidentified atom if active in the catalysis <ref name=”Structural”/>.

It was recently discovered that all antibodies contained Fab portions that catalyzed a reaction between singlet oxygen and water, yielding hydrogen peroxide, ozone, water and hydroxide radicals. Hydrogen peroxide is a toxic oxidative species and might be the product of an ancient mechanism to protect against infection. UV absorption increases the rate for this reaction. B. burgdorferi is especially vulnerable to oxidative damage because its ecological niche is in areas with limited oxygen and its genome does not encode a catalase. This oxidative mechanism might explain why some mABs are bactericidal without the use of complement. <ref name=”Structural”/>.

==References==
<references />

User:Ying Zhao/Sandbox

2012-05-03T15:19:39Z

Ying Zhao:

<ref>PMID:15713683 </ref>
<ref>[http://www.cdc.gov/lyme/stats/index.html]</ref>

==References==
<references />

User:Ying Zhao/Sandbox

2012-05-03T14:48:03Z

Ying Zhao: /* References */

<ref>PMID:15713683 </ref>

==References==
<references />

User:Ying Zhao/Sandbox

2012-04-19T17:56:31Z

Ying Zhao: New page: THIS IS YING'S SANDBOX.

THIS IS YING'S SANDBOX.

User:Ying Zhao

2012-04-19T17:56:17Z

Ying Zhao:

My name is Ying Zhao. I am an undergraduate student at Stony Brook University. I am from Stony Brook, New York, USA. I am studying Mechanical Engineering with a minor in Chemistry.

[[User:Olivia Cheng/workbench]]

[[User:Ying Zhao/Sandbox]]

User:Ying Zhao/Sandbox 2

2012-04-19T17:55:48Z

Ying Zhao: New page: THIS IS YING'S SANDBOX.

THIS IS YING'S SANDBOX.

User:Ying Zhao

2012-04-19T17:55:31Z

Ying Zhao:

User:Ying Zhao

2012-02-02T20:49:12Z

Ying Zhao:

User:Ying Zhao

2012-02-02T20:45:43Z

Ying Zhao: