A novel canonical dual computational approach for prion AGAAAAGA amyloid fibril molecular modeling
نویسندگان
چکیده
منابع مشابه
A novel canonical dual computational approach for prion AGAAAAGA amyloid fibril molecular modeling
Many experimental studies have shown that the prion AGAAAAGA palindrome hydrophobic region (113-120) has amyloid fibril forming properties and plays an important role in prion diseases. However, due to the unstable, noncrystalline and insoluble nature of the amyloid fibril, to date structural information on AGAAAAGA region (113-120) has been very limited. This region falls just within the N-ter...
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X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy are two powerful tools to determine the protein 3D structure. However, not all proteins can be successfully crystallized, particularly for membrane proteins. Although NMR spectroscopy is indeed very powerful in determining the 3D structures of membrane proteins, same as X-ray crystallography, it is still very time-consuming...
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© 2012 Zhang, licensee InTech. This is an open access chapter distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Computational Potential Energy Minimization Studies on the Prion AGAAAAGA Amyloid Fibril Mole...
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Experimental X-ray crystallography, NMR (Nuclear Magnetic Resonance) spectroscopy, dual polarization interferometry, etc are indeed very powerful tools to determine the 3-Dimensional structure of a protein (including the membrane protein); theoretical mathematical and physical computational approaches can also allow us to obtain a description of the protein 3D structure at a submicroscopic leve...
متن کاملOptimal atomic-resolution structures of prion AGAAAAGA amyloid fibrils.
X-ray crystallography is a powerful tool to determine the protein 3D structure. However, it is time-consuming and expensive, and not all proteins can be successfully crystallized, particularly for membrane proteins. Although nuclear magnetic resonance (NMR) spectroscopy is indeed a very powerful tool in determining the 3D structures of membrane proteins, it is also time-consuming and costly. To...
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ژورنال
عنوان ژورنال: Journal of Theoretical Biology
سال: 2011
ISSN: 0022-5193
DOI: 10.1016/j.jtbi.2011.06.024