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Structural Studies of SARS Virus Nsp15 and Human Innate Immunity Receptor TLR3 - 2D Crystallization and 3D Reconstruction of Biological Macromolecules: A Promising Approach for Molecular Structural Biology and Nanotechnology
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Structural Studies of SARS Virus Nsp15 and Human Innate Immunity Receptor TLR3 - 2D Crystallization and 3D Reconstruction of Biological Macromolecules: A Promising Approach for Molecular Structural Biology and Nanotechnology - Taschenbuch

2008, ISBN: 9783639063103

[ED: Taschenbuch / Paperback], [PU: VDM Verlag Dr. Müller], 3D structural determination of biological macromolecules is not only critical to understanding their mechanisms, but also essential in structural based drug discovery. Combining the high resolution imaging of TEM and efficient computer processing, protein structures in solution or in 2D crystals can be determined. Using lipid monolayer technique with Ni-NTA modified lipid, which has high affinity to 6His-tagged proteins, 2D crystal of the protein can be formed at the lipid surface. In this study, several proteins have been crystallized using this technique, including the SARS virus Nsp15 endonuclease and the human Toll-like receptor 3 extracellular domain. This approach may also have application in nanofabrication, taking advantage of the natural building bloc of proteins and virus. Single particle analysis can determine protein structures in solution without the need for crystals. 3D structures of several protein complexes had been solved by the single particle method, including IniA from Mycobacterium tuberculosis, Nsp15 and TLR3 ECD. Determining the structures of these proteins is an important step toward understanding pathogenic microbes and our immune system., [SC: 0.00], Neuware, gewerbliches Angebot, 220 mm, [GW: 195g]

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Structural Studies of SARS Virus Nsp15 and Human Innate Immunity Receptor TLR3 - Jingchuan Sun
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Structural Studies of SARS Virus Nsp15 and Human Innate Immunity Receptor TLR3 - Taschenbuch

2014, ISBN: 3639063104

ID: 20070018945

[EAN: 9783639063103], Neubuch, [PU: VDM Verlag Dr. Müller E.K. Jan 2014], Science|Life Sciences|Biological Diversity, Neuware - 3D structural determination of biological macromolecules is not only critical to understanding their mechanisms, but also essential in structural based drug discovery. Combining the high resolution imaging of TEM and efficient computer processing, protein structures in solution or in 2D crystals can be determined. Using lipid monolayer technique with Ni-NTA modified lipid, which has high affinity to 6His-tagged proteins, 2D crystal of the protein can be formed at the lipid surface. In this study, several proteins have been crystallized using this technique, including the SARS virus Nsp15 endonuclease and the human Toll-like receptor 3 extracellular domain. This approach may also have application in nanofabrication, taking advantage of the natural building bloc of proteins and virus. Single particle analysis can determine protein structures in solution without the need for crystals. 3D structures of several protein complexes had been solved by the single particle method, including IniA from Mycobacterium tuberculosis, Nsp15 and TLR3 ECD. Determining the structures of these proteins is an important step toward understanding pathogenic microbes and our immune system. 136 pp. Englisch

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Structural Studies of SARS Virus Nsp15 and Human Innate Immunity Receptor TLR3 - Jingchuan Sun
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Jingchuan Sun:
Structural Studies of SARS Virus Nsp15 and Human Innate Immunity Receptor TLR3 - Taschenbuch

2014, ISBN: 3639063104

ID: 20070035000

[EAN: 9783639063103], Neubuch, [PU: VDM Verlag Dr. Müller E.K. Jan 2014], Science|Life Sciences|Biological Diversity, Neuware - 3D structural determination of biological macromolecules is not only critical to understanding their mechanisms, but also essential in structural based drug discovery. Combining the high resolution imaging of TEM and efficient computer processing, protein structures in solution or in 2D crystals can be determined. Using lipid monolayer technique with Ni-NTA modified lipid, which has high affinity to 6His-tagged proteins, 2D crystal of the protein can be formed at the lipid surface. In this study, several proteins have been crystallized using this technique, including the SARS virus Nsp15 endonuclease and the human Toll-like receptor 3 extracellular domain. This approach may also have application in nanofabrication, taking advantage of the natural building bloc of proteins and virus. Single particle analysis can determine protein structures in solution without the need for crystals. 3D structures of several protein complexes had been solved by the single particle method, including IniA from Mycobacterium tuberculosis, Nsp15 and TLR3 ECD. Determining the structures of these proteins is an important step toward understanding pathogenic microbes and our immune system. 136 pp. Englisch

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Structural Studies of SARS Virus Nsp15 and Human Innate Immunity Receptor TLR3 - Jingchuan Sun
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Jingchuan Sun:
Structural Studies of SARS Virus Nsp15 and Human Innate Immunity Receptor TLR3 - Taschenbuch

ISBN: 9783639063103

[ED: Taschenbuch], [PU: VDM Verlag Dr. Müller e.K.], Neuware - 3D structural determination of biological macromolecules is not only critical to understanding their mechanisms, but also essential in structural based drug discovery. Combining the high resolution imaging of TEM and efficient computer processing, protein structures in solution or in 2D crystals can be determined. Using lipid monolayer technique with Ni-NTA modified lipid, which has high affinity to 6His-tagged proteins, 2D crystal of the protein can be formed at the lipid surface. In this study, several proteins have been crystallized using this technique, including the SARS virus Nsp15 endonuclease and the human Toll-like receptor 3 extracellular domain. This approach may also have application in nanofabrication, taking advantage of the natural building bloc of proteins and virus. Single particle analysis can determine protein structures in solution without the need for crystals. 3D structures of several protein complexes had been solved by the single particle method, including IniA from Mycobacterium tuberculosis, Nsp15 and TLR3 ECD. Determining the structures of these proteins is an important step toward understanding pathogenic microbes and our immune system., [SC: 0.00], Neuware, gewerbliches Angebot, 220x150x8 mm, [GW: 219g]

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2008, ISBN: 9783639063103

ID: 9643655

2D Crystallization and 3D Reconstruction of Biological Macromolecules: A Promising Approach for Molecular Structural Biology and Nanotechnology, unbekannt, Buch, [PU: VDM Verlag Dr. Müller]

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Structural Studies of SARS Virus Nsp15 and Human Innate Immunity Receptor TLR3

3D structural determination of biological macromolecules is not only critical to understanding their mechanisms, but also essential in structural based drug discovery. Combining the high resolution imaging of TEM and efficient computer processing, protein structures in solution or in 2D crystals can be determined. Using lipid monolayer technique with Ni-NTA modified lipid, which has high affinity to 6His-tagged proteins, 2D crystal of the protein can be formed at the lipid surface. In this study, several proteins have been crystallized using this technique, including the SARS virus Nsp15 endonuclease and the human Toll-like receptor 3 extracellular domain. This approach may also have application in nanofabrication, taking advantage of the natural building bloc of proteins and virus. Single particle analysis can determine protein structures in solution without the need for crystals. 3D structures of several protein complexes had been solved by the single particle method, including IniA from Mycobacterium tuberculosis, Nsp15 and TLR3 ECD. Determining the structures of these proteins is an important step toward understanding pathogenic microbes and our immune system.

Detailangaben zum Buch - Structural Studies of SARS Virus Nsp15 and Human Innate Immunity Receptor TLR3


EAN (ISBN-13): 9783639063103
ISBN (ISBN-10): 3639063104
Taschenbuch
Erscheinungsjahr: 2008
Herausgeber: VDM Verlag
132 Seiten
Gewicht: 0,213 kg
Sprache: eng/Englisch

Buch in der Datenbank seit 04.12.2008 14:16:47
Buch zuletzt gefunden am 12.04.2017 14:37:01
ISBN/EAN: 9783639063103

ISBN - alternative Schreibweisen:
3-639-06310-4, 978-3-639-06310-3


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