Cation-pi interactions: Difference between revisions

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The flat face of an aromatic ring has a partial negative charge due to the pi orbitals. Cationic sidechains (Asp, Glu) or sometimes ligands (including metal ions) often align themselves centered over the faces of aromatic rings. Over one fourth of Trp's in the Protein Data Bank interact with cations, and 99% of significant cation-pi interactions occur within a distance of 6.0 Angstroms <ref>PMID:110449714</ref>. Cation-pi interactions make a significant contribution to the overall stability of most proteins. [http://www.ncbi.nlm.nih.gov/pubmed/10449714 Gallivan and Dougherty (1999)] conclude that "cation-pi interactions should be considered alongside the more conventional hydrogen bonds, salt bridges, and hydrophobic effects in any analysis of protein structure". [http://www.umass.edu/microbio/chime/pe_beta/pe/protexpl/frntdoo2.htm Eric Martz's Protein Explorer] finds and displays potential cation-pi interactions, as described [http://www.umass.edu/microbio/chime/pe_beta/pe/protexpl/cationpi.htm here].

The flat face of an aromatic ring has a partial negative charge due to the pi orbitals. Cationic sidechains (Asp, Glu) or sometimes ligands (including metal ions) often align themselves centered over the faces of aromatic rings. Over one fourth of Trp's in the Protein Data Bank interact with cations, and 99% of significant cation-pi interactions occur within a distance of 6.0 Angstroms <ref>PMID: 110449714</ref>. Cation-pi interactions make a significant contribution to the overall stability of most proteins. [http://www.ncbi.nlm.nih.gov/pubmed/10449714 Gallivan and Dougherty (1999)] conclude that "cation-pi interactions should be considered alongside the more conventional hydrogen bonds, salt bridges, and hydrophobic effects in any analysis of protein structure". [http://www.umass.edu/microbio/chime/pe_beta/pe/protexpl/frntdoo2.htm Eric Martz's Protein Explorer] finds and displays potential cation-pi interactions, as described [http://www.umass.edu/microbio/chime/pe_beta/pe/protexpl/cationpi.htm here].

==Background==

Cation-pi interactions: Difference between revisions

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Revision as of 01:26, 20 April 2009 view source Wayne Decatur (talk \| contribs) Editor, widgeteditor 7,824 edits →Additional Literature and Resources ← Older edit		Revision as of 01:27, 20 April 2009 view source Wayne Decatur (talk \| contribs) Editor, widgeteditor 7,824 edits No edit summary Newer edit →
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	The flat face of an aromatic ring has a partial negative charge due to the pi orbitals. Cationic sidechains (Asp, Glu) or sometimes ligands (including metal ions) often align themselves centered over the faces of aromatic rings. Over one fourth of Trp's in the Protein Data Bank interact with cations, and 99% of significant cation-pi interactions occur within a distance of 6.0 Angstroms <ref>PMID:110449714</ref>. Cation-pi interactions make a significant contribution to the overall stability of most proteins. [http://www.ncbi.nlm.nih.gov/pubmed/10449714 Gallivan and Dougherty (1999)] conclude that "cation-pi interactions should be considered alongside the more conventional hydrogen bonds, salt bridges, and hydrophobic effects in any analysis of protein structure". [http://www.umass.edu/microbio/chime/pe_beta/pe/protexpl/frntdoo2.htm Eric Martz's Protein Explorer] finds and displays potential cation-pi interactions, as described [http://www.umass.edu/microbio/chime/pe_beta/pe/protexpl/cationpi.htm here].		The flat face of an aromatic ring has a partial negative charge due to the pi orbitals. Cationic sidechains (Asp, Glu) or sometimes ligands (including metal ions) often align themselves centered over the faces of aromatic rings. Over one fourth of Trp's in the Protein Data Bank interact with cations, and 99% of significant cation-pi interactions occur within a distance of 6.0 Angstroms <ref>PMID: 110449714</ref>. Cation-pi interactions make a significant contribution to the overall stability of most proteins. [http://www.ncbi.nlm.nih.gov/pubmed/10449714 Gallivan and Dougherty (1999)] conclude that "cation-pi interactions should be considered alongside the more conventional hydrogen bonds, salt bridges, and hydrophobic effects in any analysis of protein structure". [http://www.umass.edu/microbio/chime/pe_beta/pe/protexpl/frntdoo2.htm Eric Martz's Protein Explorer] finds and displays potential cation-pi interactions, as described [http://www.umass.edu/microbio/chime/pe_beta/pe/protexpl/cationpi.htm here].

	==Background==		==Background==