Ramachandran outlier

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==Ramachandran outlier==
==Ramachandran outlier==
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<StructureSection load='' size='340' side='right' caption='' scene=''>
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<StructureSection load='' size='340' side='right' caption='' scene='76/762493/1ea5_color_sec_struct/1'>
The [[Ramachandran Plot]] was described on 1963 by Ramachandran, G.N.; Ramakrishnan, C.; Sasisekharan, V. <ref>pmid 13990617</ref>
The [[Ramachandran Plot]] was described on 1963 by Ramachandran, G.N.; Ramakrishnan, C.; Sasisekharan, V. <ref>pmid 13990617</ref>
Ramachandran outlier are those aminoacids with non favorable dihedral angles, and Ramachandran plot is a powerful tool for making those evident. Most of the times, Ramachandran outliers are a consequence of mistakes during the data processing.
Ramachandran outlier are those aminoacids with non favorable dihedral angles, and Ramachandran plot is a powerful tool for making those evident. Most of the times, Ramachandran outliers are a consequence of mistakes during the data processing.
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However, sometimes, Ramachandran outliers might play a special role in the structure function. See for example the case of Ser-200 in the structure <scene name='76/762493/1ea5_color_sec_struct/1'>1ea5</scene>. Let's draw the <jmol><jmolLink><script>ramachandran</script><text>Ramachandran Plot</text></jmolLink></jmol>
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However, sometimes, Ramachandran outliers might play a special role in the structure function. See for example the case of Ser-200 in the structure <scene name='76/762493/1ea5_color_sec_struct/1'>1ea5</scene>. Let's draw the <jmol><jmolLink><script>plot ramachandran</script><text>Ramachandran Plot</text></jmolLink></jmol>.
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Notice that the residues in <jmol><jmolLink><script>display beta</script><text>beta sheets</text></jmolLink></jmol> are colored in yellow, and the residues in <jmol><jmolLink><script>display beta</script><text>alpha helix</text></jmolLink></jmol> colored in magenta.

Revision as of 16:09, 13 August 2017

Ramachandran outlier

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References

  1. RAMACHANDRAN GN, RAMAKRISHNAN C, SASISEKHARAN V. Stereochemistry of polypeptide chain configurations. J Mol Biol. 1963 Jul;7:95-9. PMID:13990617

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