Mahalia Serrano/Sandbox1 - Revision history

Mahalia Serrano at 04:47, 4 December 2014

2014-12-04T04:47:43Z

←Older revision		Revision as of 04:47, 4 December 2014
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	== Structure ==		== Structure ==

-	HSA exists as a monomer that is comprised mostly of alpha helices ~~that form several hydrophobic binding pockets throughout the molecule~~. Each of the <scene name='57/571397/Different_domains/1'>three homologous helical domains</scene>	+	HSA exists as a monomer that is comprised mostly of alpha helices. Each of the <scene name='57/571397/Different_domains/1'>three homologous helical domains</scene>
	(<B><font color="purple">domain I</font></B>, <B><font color="orange">domain II</font></B>, <B><font color="green">domain III</font></B>)		(<B><font color="purple">domain I</font></B>, <B><font color="orange">domain II</font></B>, <B><font color="green">domain III</font></B>)
-	are further divided into subdomains A and B (A=darker shade, B=lighter shade)	+	are further divided into subdomains A and B (A=darker shade, B=lighter shade), which form several hydrophobic pockets throughout the molecule.

Mahalia Serrano at 04:29, 4 December 2014

2014-12-04T04:29:42Z

←Older revision		Revision as of 04:29, 4 December 2014
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	HSA exists as a monomer that is comprised mostly of alpha helices that form several hydrophobic binding pockets throughout the molecule. Each of the <scene name='57/571397/Different_domains/1'>three homologous helical domains</scene>		HSA exists as a monomer that is comprised mostly of alpha helices that form several hydrophobic binding pockets throughout the molecule. Each of the <scene name='57/571397/Different_domains/1'>three homologous helical domains</scene>
-	(<B><font color="purple">IA</font></B>, <B><font color="~~light purple~~">IB</font></B>	+	(<B><font color="purple">domain I</font></B>, <B><font color="orange">domain II</font></B>, <B><font color="green">domain III</font></B>)
	are further divided into subdomains A and B (A=darker shade, B=lighter shade)		are further divided into subdomains A and B (A=darker shade, B=lighter shade)

Mahalia Serrano at 04:27, 4 December 2014

2014-12-04T04:27:56Z

←Older revision		Revision as of 04:27, 4 December 2014
Line 8:		Line 8:
	== Structure ==		== Structure ==

-	HSA exists as a monomer that is comprised mostly of alpha helices that form several hydrophobic binding pockets throughout the molecule. Each of the three homologous helical domains are further divided into subdomains A and B (A=darker shade, B=lighter shade)	+	HSA exists as a monomer that is comprised mostly of alpha helices that form several hydrophobic binding pockets throughout the molecule. Each of the <scene name='57/571397/Different_domains/1'>three homologous helical domains</scene>
		+	(<B><font color="purple">IA</font></B>, <B><font color="light purple">IB</font></B>
		+	are further divided into subdomains A and B (A=darker shade, B=lighter shade)
		+

-	<scene name='57/571397/Different_domains/1'>subdomains: IA, IB, IIA, IIB, IIIA, IIIB</scene>

Mahalia Serrano at 04:20, 4 December 2014

2014-12-04T04:20:24Z

←Older revision		Revision as of 04:20, 4 December 2014
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	== Structure ==		== Structure ==

-	HSA exists as a monomer that is comprised mostly of ~~<scene name='57/571397/Alpha_helices/1'>~~alpha helices~~</scene>~~ that form several hydrophobic binding pockets throughout the molecule. Each of the three homologous helical domains are further divided into subdomains A and B (A=darker shade, B=lighter shade)	+	HSA exists as a monomer that is comprised mostly of alpha helices that form several hydrophobic binding pockets throughout the molecule. Each of the three homologous helical domains are further divided into subdomains A and B (A=darker shade, B=lighter shade)

	<scene name='57/571397/Different_domains/1'>subdomains: IA, IB, IIA, IIB, IIIA, IIIB</scene>		<scene name='57/571397/Different_domains/1'>subdomains: IA, IB, IIA, IIB, IIIA, IIIB</scene>
		+
		+
		+
		+	== Function ==
		+

	Being the major protein in blood, it functions to maintain the osmotic pressure and the pH of the blood. But most importantly, it functions to transport various substances through the bloodstream. HSA does not carry a specific cargo, although it does have preference for fat-soluble substances as it can bury the water-insoluble molecules into its hydrophobic core. Here, we can see <scene name='57/571397/Hsa_with_myr_and_aspirin/5'>HSA with both myristate (a fatty acid, shown in grey spheres) and aspirin (a common analgesic, shown in pink) bound</scene> to its hydrophobic pockets. HSA transports a wide variety of substances through the bloodstream including carbohydrates (e.g <scene name='57/571397/Hsa_with_glucose/6'>glucose</scene>), fatty acids (e.g. <scene name='57/571397/Hsa_with_arachidonic_acid/3'>arachidonic acid</scene>), hormones (e.g. <scene name='57/571397/Hsa_with_thyroxine/6'>thyroxine</scene>, a thyroid hormone), and drugs (e.g. <scene name='57/571397/Hsa_with_ibp/1'>ibuprofen</scene>, an anti-inflammatory drug).		Being the major protein in blood, it functions to maintain the osmotic pressure and the pH of the blood. But most importantly, it functions to transport various substances through the bloodstream. HSA does not carry a specific cargo, although it does have preference for fat-soluble substances as it can bury the water-insoluble molecules into its hydrophobic core. Here, we can see <scene name='57/571397/Hsa_with_myr_and_aspirin/5'>HSA with both myristate (a fatty acid, shown in grey spheres) and aspirin (a common analgesic, shown in pink) bound</scene> to its hydrophobic pockets. HSA transports a wide variety of substances through the bloodstream including carbohydrates (e.g <scene name='57/571397/Hsa_with_glucose/6'>glucose</scene>), fatty acids (e.g. <scene name='57/571397/Hsa_with_arachidonic_acid/3'>arachidonic acid</scene>), hormones (e.g. <scene name='57/571397/Hsa_with_thyroxine/6'>thyroxine</scene>, a thyroid hormone), and drugs (e.g. <scene name='57/571397/Hsa_with_ibp/1'>ibuprofen</scene>, an anti-inflammatory drug).

	Because HSA is very abundant in blood serum, most biomarker studies involving serum requires preliminary removal of HSA so that other non-abundant but otherwise important disease-indicating proteins can be detected. In our group, we exploit several properties of HSA in order to efficiently remove it from serum prior to biomarker analysis. These properties include its low isoelectric point (pI of about 4.7) due to a number of <scene name='57/571397/Overall_structure_of_hsa/5'>acidic residues</scene>, and its tendency to bind hydrophobic molecules through its hydrophobic pockets.		Because HSA is very abundant in blood serum, most biomarker studies involving serum requires preliminary removal of HSA so that other non-abundant but otherwise important disease-indicating proteins can be detected. In our group, we exploit several properties of HSA in order to efficiently remove it from serum prior to biomarker analysis. These properties include its low isoelectric point (pI of about 4.7) due to a number of <scene name='57/571397/Overall_structure_of_hsa/5'>acidic residues</scene>, and its tendency to bind hydrophobic molecules through its hydrophobic pockets.

Mahalia Serrano at 23:34, 3 December 2014

2014-12-03T23:34:36Z

←Older revision		Revision as of 23:34, 3 December 2014
Line 8:		Line 8:
	== Structure ==		== Structure ==

-	HSA exists as a monomer that is comprised mostly of ~~homologous~~ <scene name='57/571397/Alpha_helices/1'>alpha helices</scene> that form several hydrophobic binding pockets throughout the molecule.	+	HSA exists as a monomer that is comprised mostly of <scene name='57/571397/Alpha_helices/1'>alpha helices</scene> that form several hydrophobic binding pockets throughout the molecule. Each of the three homologous helical domains are further divided into subdomains A and B (A=darker shade, B=lighter shade)

	<scene name='57/571397/Different_domains/1'>subdomains: IA, IB, IIA, IIB, IIIA, IIIB</scene>		<scene name='57/571397/Different_domains/1'>subdomains: IA, IB, IIA, IIB, IIIA, IIIB</scene>

Mahalia Serrano at 23:24, 3 December 2014

2014-12-03T23:24:58Z

←Older revision		Revision as of 23:24, 3 December 2014
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-	== ~~test~~ ==	+	== '''HUMAN SERUM ALBUMIN (HSA)''' ==

-	~~This is a~~ <scene ~~name~~='~~57/571388/Test/1~~'~~>test<~~/~~scene~~>.	+	<Structure load='4K2C_all_domains_v2.pdb' size='500' frame='true' align='right' caption='Human serum albumin (PDB code [[4iw1]])' scene='Insert optional scene name here' />

-	</~~StructureSection~~>	+	'''Human serum albumin''' (HSA) is the most abundant protein in the blood plasma, amounting to about 35 to 50 grams per liter of serum. With a molecular weight of about 66.5 kDa, it functions mainly to maintain the pH and osmotic pressure of the blood and to transport a wide variety of endogenous and exogenous substances.
		+
		+
		+	== Structure ==
		+
		+	HSA exists as a monomer that is comprised mostly of homologous <scene name='57/571397/Alpha_helices/1'>alpha helices</scene> that form several hydrophobic binding pockets throughout the molecule.
		+
		+	<scene name='57/571397/Different_domains/1'>subdomains: IA, IB, IIA, IIB, IIIA, IIIB</scene>
		+
		+	Being the major protein in blood, it functions to maintain the osmotic pressure and the pH of the blood. But most importantly, it functions to transport various substances through the bloodstream. HSA does not carry a specific cargo, although it does have preference for fat-soluble substances as it can bury the water-insoluble molecules into its hydrophobic core. Here, we can see <scene name='57/571397/Hsa_with_myr_and_aspirin/5'>HSA with both myristate (a fatty acid, shown in grey spheres) and aspirin (a common analgesic, shown in pink) bound</scene> to its hydrophobic pockets. HSA transports a wide variety of substances through the bloodstream including carbohydrates (e.g <scene name='57/571397/Hsa_with_glucose/6'>glucose</scene>), fatty acids (e.g. <scene name='57/571397/Hsa_with_arachidonic_acid/3'>arachidonic acid</scene>), hormones (e.g. <scene name='57/571397/Hsa_with_thyroxine/6'>thyroxine</scene>, a thyroid hormone), and drugs (e.g. <scene name='57/571397/Hsa_with_ibp/1'>ibuprofen</scene>, an anti-inflammatory drug).
		+
		+	Because HSA is very abundant in blood serum, most biomarker studies involving serum requires preliminary removal of HSA so that other non-abundant but otherwise important disease-indicating proteins can be detected. In our group, we exploit several properties of HSA in order to efficiently remove it from serum prior to biomarker analysis. These properties include its low isoelectric point (pI of about 4.7) due to a number of <scene name='57/571397/Overall_structure_of_hsa/5'>acidic residues</scene>, and its tendency to bind hydrophobic molecules through its hydrophobic pockets.

Mahalia Serrano at 18:41, 7 December 2013

2013-12-07T18:41:07Z

←Older revision		Revision as of 18:41, 7 December 2013
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	== test ==		== test ==
-	~~<StructureSection load='1dq8' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' scene=''>~~	+
	This is a <scene name='57/571388/Test/1'>test</scene>.		This is a <scene name='57/571388/Test/1'>test</scene>.

	</StructureSection>		</StructureSection>

Mahalia Serrano at 05:00, 7 December 2013

2013-12-07T05:00:36Z

←Older revision		Revision as of 05:00, 7 December 2013
Line 1:		Line 1:
	== test ==		== test ==
	<StructureSection load='1dq8' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' scene=''>		<StructureSection load='1dq8' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' scene=''>
-	~~Anything in this section will appear adjacent to the 3D structure and will be scrollable~~.	+	This is a <scene name='57/571388/Test/1'>test</scene>.

	</StructureSection>		</StructureSection>
-
-	This is a <scene name='57/571388/Test/1'>test</scene>.

Mahalia Serrano at 04:59, 7 December 2013

2013-12-07T04:59:43Z

←Older revision		Revision as of 04:59, 7 December 2013
Line 1:		Line 1:
-	== ~~Your Heading Here (maybe something like 'Structure')~~ ==	+	== test ==
	<StructureSection load='1dq8' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' scene=''>		<StructureSection load='1dq8' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' scene=''>
	Anything in this section will appear adjacent to the 3D structure and will be scrollable.		Anything in this section will appear adjacent to the 3D structure and will be scrollable.

	</StructureSection>		</StructureSection>
		+
		+	This is a <scene name='57/571388/Test/1'>test</scene>.

Mahalia Serrano: New page: == Your Heading Here (maybe something like 'Structure') == Any...

2013-12-07T04:51:26Z

New page: == Your Heading Here (maybe something like 'Structure') == <StructureSection load='1dq8' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry 1dq8)' scene=''> Any...

New page

== Your Heading Here (maybe something like 'Structure') ==
<StructureSection load='1dq8' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' scene=''>
Anything in this section will appear adjacent to the 3D structure and will be scrollable.

</StructureSection>