Sandbox Reserved 479 - Revision history

Nishika Patel: /* X-Ray Crystallography and Scattering */

Nishika Patel — Wed, 02 May 2012 22:47:57 GMT

X-Ray Crystallography and Scattering

←Older revision		Revision as of 22:47, 2 May 2012
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	====X-Ray Crystallography and Scattering====		====X-Ray Crystallography and Scattering====

-	It was not until recently that crystal structures could be used to analyze myosin and it's role in the actinomysin chemomechanical cycle. X-ray diffraction studies have been conducted on whole muscles and muscle fibers to learn how structural changes promote and facilitate motor activity. Modern synchrotron radiation sources allow us to study myosin at the molecular level under near-physiological conditions. Muscle cells exhibit low scattering power in X-ray images, however, so a clear crystalline structure cannot not form. A flat detector is needed because reflections are concentrated in the low angle regions. Snychrotron radiation generates a monochromatic X-ray breams of diameter 0.2-0.3 mm, similar to that of the muscle fiber, and making high resolution images and video of a single muscle cell possible via x-ray scattering patterns.<ref name="Koubassova">PMID: 22339600</ref>	+	It was not until recently that crystal structures could be used to analyze myosin and it's role in the actinomysin chemomechanical cycle. X-ray diffraction studies have been conducted on whole muscles and muscle fibers to learn how structural changes promote and facilitate motor activity. Modern synchrotron radiation sources allow us to study myosin at the molecular level under near-physiological conditions. Muscle cells exhibit low scattering power in X-ray images, however, so a clear crystalline structure cannot not form. A flat detector is needed because reflections are concentrated in the low angle regions. Snychrotron radiation generates a monochromatic X-ray breams of diameter 0.2-0.3 mm, similar to that of the muscle fiber, and making high resolution images and video of a single muscle cell possible via x-ray scattering patterns. New technology using snychrotron radiation and 2 dimensional detectors will allow researchers to gain even more insight into the structure of myosin and it's interaction with actin in unique time and spatial resolution.<ref name="Koubassova">PMID: 22339600</ref>

	==Interaction with Actin==		==Interaction with Actin==

Nishika Patel: /* X-Ray Crystallography and Scattering */

Nishika Patel — Wed, 02 May 2012 22:44:12 GMT

X-Ray Crystallography and Scattering

←Older revision		Revision as of 22:44, 2 May 2012
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	====X-Ray Crystallography and Scattering====		====X-Ray Crystallography and Scattering====

-	It was not until recently that crystal structures could be used to analyze myosin and it's role in the actinomysin chemomechanical cycle. X-ray diffraction studies have been conducted on whole muscles and muscle fibers to learn how structural changes promote and facilitate motor activity. ~~Movement of~~ myosin ~~was analyzed~~ under near physiological conditions ~~using modern synchrotron radiation sources. Structural alterations were created through use of unique time and spatial resolution~~. Muscle cells exhibit low scattering power in X-ray images, so a clear crystalline structure cannot not form. A flat detector is needed because reflections are concentrated in the low angle regions. Snychrotron radiation generates a monochromatic X-ray breams of diameter 0.2-0.3 mm, similar to that of the muscle fiber, and making high resolution images and video of a single muscle cell possible.<ref name="Koubassova">PMID: 22339600</ref>	+	It was not until recently that crystal structures could be used to analyze myosin and it's role in the actinomysin chemomechanical cycle. X-ray diffraction studies have been conducted on whole muscles and muscle fibers to learn how structural changes promote and facilitate motor activity. Modern synchrotron radiation sources allow us to study myosin at the molecular level under near-physiological conditions. Muscle cells exhibit low scattering power in X-ray images, however, so a clear crystalline structure cannot not form. A flat detector is needed because reflections are concentrated in the low angle regions. Snychrotron radiation generates a monochromatic X-ray breams of diameter 0.2-0.3 mm, similar to that of the muscle fiber, and making high resolution images and video of a single muscle cell possible via x-ray scattering patterns.<ref name="Koubassova">PMID: 22339600</ref>

	==Interaction with Actin==		==Interaction with Actin==

Nishika Patel: /* Structure */

Nishika Patel — Wed, 02 May 2012 22:29:09 GMT

Structure

←Older revision		Revision as of 22:29, 2 May 2012
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	==Structure==		==Structure==

-	Myosin is a 520 kDa hexamer, or a '''hexa-oligomer''' (6 subunit) structure. It is comprised of two heavy chains (weighing 220 kDa each) and 4 light chains (weighing 20 kDa each).<ref name="CHEM43">[http://www.cs.stedwards.edu/chem/Chemistry/CHEM43/CHEM43/Myosin/STRUCT~1.HTM]</ref> The hexamer's 2 identical heavy chains connected via the coiled coil structure, and each containing a regulatory and essential light chain (total of 4). The 2-D structure below of myosin II shows 7 stranded <scene name='Sandbox_Reserved_479/2mys_beta_sheet/2'>beta sheet</scene> (Jmol) and the ATP-binding site between the middle and N-terminal of the protein. The C-terminal contains the light chains (regulatory domain) and acts as the lever arm to enhance the converter domain's rotational movements.<ref name="sampath">[http://www.sampath.koppole.com/research.htm]</ref>	+	Myosin is a 520 kDa hexamer, or a '''hexa-oligomer''' (6 subunit) structure. It is comprised of two heavy chains (weighing 220 kDa each) and 4 light chains (weighing 20 kDa each).<ref name="CHEM43">[http://www.cs.stedwards.edu/chem/Chemistry/CHEM43/CHEM43/Myosin/STRUCT~1.HTM]</ref> The hexamer's 2 identical heavy chains connected via the coiled coil structure, and each containing a regulatory and essential light chain (total of 4). The 2-D structure below of myosin II head shows 7 stranded <scene name='Sandbox_Reserved_479/2mys_beta_sheet/2'>beta sheet</scene> (Jmol) and the ATP-binding site between the middle and N-terminal of the protein. The C-terminal contains the light chains (regulatory domain) and acts as the lever arm to enhance the converter domain's rotational movements.<ref name="sampath">[http://www.sampath.koppole.com/research.htm]</ref>

	[[Image:Mds1.png]]		[[Image:Mds1.png]]

Nishika Patel: /* Mechanism of Action */

Nishika Patel — Wed, 02 May 2012 22:27:43 GMT

Mechanism of Action

←Older revision		Revision as of 22:27, 2 May 2012
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	Myosin disassociates and binds to actin via the hydrolysis of ATP into ADP and Pi. The force behind a muscle contraction is due to the swinging lever arm (myosin).<ref name="esrf">[http://www.esrf.eu/UsersAndScience/Publications/Highlights/2003/MX/MX03]</ref>		Myosin disassociates and binds to actin via the hydrolysis of ATP into ADP and Pi. The force behind a muscle contraction is due to the swinging lever arm (myosin).<ref name="esrf">[http://www.esrf.eu/UsersAndScience/Publications/Highlights/2003/MX/MX03]</ref>

-	==Mechanism of Action==	+	===Mechanism of Action===

	Myosin plays a role in the universal mechanism known as the actinomysin chemomechanical cycle. Actin binds and releases myosin, causing the myosin lever to interact and relax in a cyclic manner.<ref name="legacy">[http://legacy.owensboro.kctcs.edu/gcaplan/anat/notes/api%20notes%20j%20%20muscle%20contraction.htm]</ref>		Myosin plays a role in the universal mechanism known as the actinomysin chemomechanical cycle. Actin binds and releases myosin, causing the myosin lever to interact and relax in a cyclic manner.<ref name="legacy">[http://legacy.owensboro.kctcs.edu/gcaplan/anat/notes/api%20notes%20j%20%20muscle%20contraction.htm]</ref>

Nishika Patel: /* Interaction with Actin */

Nishika Patel — Wed, 02 May 2012 22:27:13 GMT

Interaction with Actin

←Older revision		Revision as of 22:27, 2 May 2012
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	[[Image:actinandmyosin.png]]		[[Image:actinandmyosin.png]]

-	Myosin ~~disassociating~~ and ~~binding~~ to actin via the hydrolysis of ATP into ADP and Pi. The force behind a muscle contraction is due to the swinging lever arm (myosin).<ref name="esrf">[http://www.esrf.eu/UsersAndScience/Publications/Highlights/2003/MX/MX03]</ref>	+	Myosin disassociates and binds to actin via the hydrolysis of ATP into ADP and Pi. The force behind a muscle contraction is due to the swinging lever arm (myosin).<ref name="esrf">[http://www.esrf.eu/UsersAndScience/Publications/Highlights/2003/MX/MX03]</ref>

	==Mechanism of Action==		==Mechanism of Action==

Nishika Patel: /* Interaction with Actin */

Nishika Patel — Wed, 02 May 2012 22:26:43 GMT

Interaction with Actin

←Older revision		Revision as of 22:26, 2 May 2012
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	[[Image:actinandmyosin.png]]		[[Image:actinandmyosin.png]]
		+
	Myosin disassociating and binding to actin via the hydrolysis of ATP into ADP and Pi. The force behind a muscle contraction is due to the swinging lever arm (myosin).<ref name="esrf">[http://www.esrf.eu/UsersAndScience/Publications/Highlights/2003/MX/MX03]</ref>		Myosin disassociating and binding to actin via the hydrolysis of ATP into ADP and Pi. The force behind a muscle contraction is due to the swinging lever arm (myosin).<ref name="esrf">[http://www.esrf.eu/UsersAndScience/Publications/Highlights/2003/MX/MX03]</ref>

Nishika Patel: /* Interaction with Actin[http://www.esrf.eu/UsersAndScience/Publications/Highlights/2003/MX/MX03] */

Nishika Patel — Wed, 02 May 2012 22:26:23 GMT

Interaction with Actin<ref name="esrf">[http://www.esrf.eu/UsersAndScience/Publications/Highlights/2003/MX/MX03]</ref>

←Older revision		Revision as of 22:26, 2 May 2012
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	It was not until recently that crystal structures could be used to analyze myosin and it's role in the actinomysin chemomechanical cycle. X-ray diffraction studies have been conducted on whole muscles and muscle fibers to learn how structural changes promote and facilitate motor activity. Movement of myosin was analyzed under near physiological conditions using modern synchrotron radiation sources. Structural alterations were created through use of unique time and spatial resolution. Muscle cells exhibit low scattering power in X-ray images, so a clear crystalline structure cannot not form. A flat detector is needed because reflections are concentrated in the low angle regions. Snychrotron radiation generates a monochromatic X-ray breams of diameter 0.2-0.3 mm, similar to that of the muscle fiber, and making high resolution images and video of a single muscle cell possible.<ref name="Koubassova">PMID: 22339600</ref>		It was not until recently that crystal structures could be used to analyze myosin and it's role in the actinomysin chemomechanical cycle. X-ray diffraction studies have been conducted on whole muscles and muscle fibers to learn how structural changes promote and facilitate motor activity. Movement of myosin was analyzed under near physiological conditions using modern synchrotron radiation sources. Structural alterations were created through use of unique time and spatial resolution. Muscle cells exhibit low scattering power in X-ray images, so a clear crystalline structure cannot not form. A flat detector is needed because reflections are concentrated in the low angle regions. Snychrotron radiation generates a monochromatic X-ray breams of diameter 0.2-0.3 mm, similar to that of the muscle fiber, and making high resolution images and video of a single muscle cell possible.<ref name="Koubassova">PMID: 22339600</ref>

-	==Interaction with Actin~~<ref name="esrf">[http://www.esrf.eu/UsersAndScience/Publications/Highlights/2003/MX/MX03]</ref>~~==	+	==Interaction with Actin==

	[[Image:actinandmyosin.png]]		[[Image:actinandmyosin.png]]
		+	Myosin disassociating and binding to actin via the hydrolysis of ATP into ADP and Pi. The force behind a muscle contraction is due to the swinging lever arm (myosin).<ref name="esrf">[http://www.esrf.eu/UsersAndScience/Publications/Highlights/2003/MX/MX03]</ref>

	==Mechanism of Action==		==Mechanism of Action==

Nishika Patel: /* X-Ray Crystallography and Scattering */

Nishika Patel — Wed, 02 May 2012 22:20:06 GMT

X-Ray Crystallography and Scattering

←Older revision		Revision as of 22:20, 2 May 2012
Line 27:		Line 27:
	It was not until recently that crystal structures could be used to analyze myosin and it's role in the actinomysin chemomechanical cycle. X-ray diffraction studies have been conducted on whole muscles and muscle fibers to learn how structural changes promote and facilitate motor activity. Movement of myosin was analyzed under near physiological conditions using modern synchrotron radiation sources. Structural alterations were created through use of unique time and spatial resolution. Muscle cells exhibit low scattering power in X-ray images, so a clear crystalline structure cannot not form. A flat detector is needed because reflections are concentrated in the low angle regions. Snychrotron radiation generates a monochromatic X-ray breams of diameter 0.2-0.3 mm, similar to that of the muscle fiber, and making high resolution images and video of a single muscle cell possible.<ref name="Koubassova">PMID: 22339600</ref>		It was not until recently that crystal structures could be used to analyze myosin and it's role in the actinomysin chemomechanical cycle. X-ray diffraction studies have been conducted on whole muscles and muscle fibers to learn how structural changes promote and facilitate motor activity. Movement of myosin was analyzed under near physiological conditions using modern synchrotron radiation sources. Structural alterations were created through use of unique time and spatial resolution. Muscle cells exhibit low scattering power in X-ray images, so a clear crystalline structure cannot not form. A flat detector is needed because reflections are concentrated in the low angle regions. Snychrotron radiation generates a monochromatic X-ray breams of diameter 0.2-0.3 mm, similar to that of the muscle fiber, and making high resolution images and video of a single muscle cell possible.<ref name="Koubassova">PMID: 22339600</ref>

-	==Interaction with Actin==<ref name="esrf">[http://www.esrf.eu/UsersAndScience/Publications/Highlights/2003/MX/MX03]</ref>	+	==Interaction with Actin<ref name="esrf">[http://www.esrf.eu/UsersAndScience/Publications/Highlights/2003/MX/MX03]</ref>==

	[[Image:actinandmyosin.png]]		[[Image:actinandmyosin.png]]

Nishika Patel: /* Interaction with Actin */

Nishika Patel — Wed, 02 May 2012 22:19:33 GMT

Interaction with Actin

←Older revision		Revision as of 22:19, 2 May 2012
Line 27:		Line 27:
	It was not until recently that crystal structures could be used to analyze myosin and it's role in the actinomysin chemomechanical cycle. X-ray diffraction studies have been conducted on whole muscles and muscle fibers to learn how structural changes promote and facilitate motor activity. Movement of myosin was analyzed under near physiological conditions using modern synchrotron radiation sources. Structural alterations were created through use of unique time and spatial resolution. Muscle cells exhibit low scattering power in X-ray images, so a clear crystalline structure cannot not form. A flat detector is needed because reflections are concentrated in the low angle regions. Snychrotron radiation generates a monochromatic X-ray breams of diameter 0.2-0.3 mm, similar to that of the muscle fiber, and making high resolution images and video of a single muscle cell possible.<ref name="Koubassova">PMID: 22339600</ref>		It was not until recently that crystal structures could be used to analyze myosin and it's role in the actinomysin chemomechanical cycle. X-ray diffraction studies have been conducted on whole muscles and muscle fibers to learn how structural changes promote and facilitate motor activity. Movement of myosin was analyzed under near physiological conditions using modern synchrotron radiation sources. Structural alterations were created through use of unique time and spatial resolution. Muscle cells exhibit low scattering power in X-ray images, so a clear crystalline structure cannot not form. A flat detector is needed because reflections are concentrated in the low angle regions. Snychrotron radiation generates a monochromatic X-ray breams of diameter 0.2-0.3 mm, similar to that of the muscle fiber, and making high resolution images and video of a single muscle cell possible.<ref name="Koubassova">PMID: 22339600</ref>

-	==Interaction with Actin==	+	==Interaction with Actin==<ref name="esrf">[http://www.esrf.eu/UsersAndScience/Publications/Highlights/2003/MX/MX03]</ref>

-	[[Image:actinandmyosin.png]]~~<ref name="esrf">[http://www.esrf.eu/UsersAndScience/Publications/Highlights/2003/MX/MX03]</ref>~~	+	[[Image:actinandmyosin.png]]

	==Mechanism of Action==		==Mechanism of Action==

Nishika Patel: /* Interaction with Actin */

Nishika Patel — Wed, 02 May 2012 22:17:01 GMT

Interaction with Actin

←Older revision		Revision as of 22:17, 2 May 2012
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	==Interaction with Actin==		==Interaction with Actin==

-	[[Image:~~fig023~~.png]]<ref name="esrf">[http://www.esrf.eu/UsersAndScience/Publications/Highlights/2003/MX/MX03]</ref>	+	[[Image:actinandmyosin.png]]<ref name="esrf">[http://www.esrf.eu/UsersAndScience/Publications/Highlights/2003/MX/MX03]</ref>

	==Mechanism of Action==		==Mechanism of Action==