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Three-dimensional structure of alpha...
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Tang, Jinghua.
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Three-dimensional structure of alpha-actinin from Cryo-EM reconstruction.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
Three-dimensional structure of alpha-actinin from Cryo-EM reconstruction./
作者:
Tang, Jinghua.
面頁冊數:
128 p.
附註:
Source: Dissertation Abstracts International, Volume: 61-07, Section: B, page: 3466.
Contained By:
Dissertation Abstracts International61-07B.
標題:
Biophysics, General. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9980759
ISBN:
0599869909
Three-dimensional structure of alpha-actinin from Cryo-EM reconstruction.
Tang, Jinghua.
Three-dimensional structure of alpha-actinin from Cryo-EM reconstruction.
- 128 p.
Source: Dissertation Abstracts International, Volume: 61-07, Section: B, page: 3466.
Thesis (Ph.D.)--The Florida State University, 2000.
A combination of cryoelectron microscopy 3D reconstruction, x-ray crystallography, nuclear magnetic resonance spectroscopy and homology modeling methods was applied to structural studies of the actin crosslinking protein alpha-actinin alpha-actinin was induced to form 2D array on a lipid monolayer. After collecting electron images from the frozen hydrated specimen of the 2D crystals, image processing was carried out to reconstruct a 3D structure of the alpha-actinin molecule. In order to better interpret the intermediate resolution 3D structure, molecular modeling procedure was used to construct a molecular model of the whole molecule by combining various domain models, which are built by homology modeling against existing atomic structures.
ISBN: 0599869909Subjects--Topical Terms:
1019105
Biophysics, General.
Three-dimensional structure of alpha-actinin from Cryo-EM reconstruction.
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Source: Dissertation Abstracts International, Volume: 61-07, Section: B, page: 3466.
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A combination of cryoelectron microscopy 3D reconstruction, x-ray crystallography, nuclear magnetic resonance spectroscopy and homology modeling methods was applied to structural studies of the actin crosslinking protein alpha-actinin alpha-actinin was induced to form 2D array on a lipid monolayer. After collecting electron images from the frozen hydrated specimen of the 2D crystals, image processing was carried out to reconstruct a 3D structure of the alpha-actinin molecule. In order to better interpret the intermediate resolution 3D structure, molecular modeling procedure was used to construct a molecular model of the whole molecule by combining various domain models, which are built by homology modeling against existing atomic structures.
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After building an initial model, the model was docked into the electron microscopy reconstruction. Both qualitative and quantitative comparison between the model and the cryoelectron microscopy reconstruction were carried out to improve the fitting of the model to the experimental reconstruction.
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The refined molecular model of the alpha-actinin provides the first view of the overall structure of a complete actin cross-linking protein. The close proximity between the C-terminal calmodulin-like domain and the actin binding domain provides an explanation on the involvement of the C-terminal domain in the actin binding of alpha-actinin and a possible mechanism in the regulation of calcium sensitive alpha-actinin isoforms.
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http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=9980759
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