Difference between revisions of "Fabry:Normal mode analysis"
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| + | Maybe one of the first questions that can be asked in this task is, why we use ''low-frequency'' normal modes. This is explained in the paper of Marc Delarue and Philippe Dumas<ref>Marc Delarue and Philippe Dumas '''[http://www.pnas.org/content/101/18/6957.full.pdf On the use of low-frequency normal modes to enforce collective movements in refining macromolecular structural models]''', Proc. Natl. Acad. Sci. (USA), 101, 6957-6962 (2004)</ref>, where they claim, that |
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| + | Why do we use low frequency |
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== WEBnm@ == |
== WEBnm@ == |
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</figtable> |
</figtable> |
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</div> |
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| + | == References == |
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| + | <references/> |
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Revision as of 14:24, 5 July 2012
Maybe one of the first questions that can be asked in this task is, why we use low-frequency normal modes. This is explained in the paper of Marc Delarue and Philippe Dumas<ref>Marc Delarue and Philippe Dumas On the use of low-frequency normal modes to enforce collective movements in refining macromolecular structural models, Proc. Natl. Acad. Sci. (USA), 101, 6957-6962 (2004)</ref>, where they claim, that
Why do we use low frequency
WEBnm@
<figtable id="tab:webnma_3hg2">
In this table are the 6 modes shown, that were calculated by WEBnm@. Depicted is the structure 3HG2, which represents the Human α-galactosidase catalytic mechanism with empty active site in cyan and the substrate binding site at position 203 to 207 highlighted in red.
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</figtable>
<figtable id="tab:webnma_3hg3"> In this table are the 6 modes shown, that were calculated by WEBnm@. Depicted is the structure 3HG3, which represents the Human α-galactosidase catalytic mechanism with bound substrate (green, α-D-Galactose with bound α-D-Glucose) in cyan and the substrate binding site at position 203 to 207 highlighted in red.
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</figtable>
References
<references/>
