Salt bridges: Difference between revisions

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<applet load='1cbr' size='300' frame='true' align='right' caption='Salt bridge between retinoic acid(-) and arg131(+) in 1cbr.'
<applet load='1cbr' size='300' frame='true' align='right' caption='Salt bridge between retinoic acid(-) and arg131(+) in [[1cbr]].'
scene='Salt_bridges/Salt_bridge/1' />
scene='Salt_bridges/Salt_bridge/1' />
In proteins, salt bridges occur between amino acid side-chains with opposite positive or negative full-electron charges, namely, (at neutral pH) Glu- or Asp- vs. Arg+ or Lys+. They may also occur between ionized organic ligands, such as acetylcholine+ (or example at right: [[1cbr]]), or inorganic ions, such as K+ or Cl-, and amino acid side-chains.
In proteins, salt bridges occur between amino acid side-chains with opposite positive or negative full-electron charges, namely, (at neutral pH) Glu- or Asp- vs. Arg+ or Lys+. They may also occur between ionized organic ligands, such as acetylcholine+ (or example at right: [[1cbr]]), or inorganic ions, such as K+ or Cl-, and amino acid side-chains.

Revision as of 20:53, 22 April 2012

Salt bridge between retinoic acid(-) and arg131(+) in 1cbr.

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In proteins, salt bridges occur between amino acid side-chains with opposite positive or negative full-electron charges, namely, (at neutral pH) Glu- or Asp- vs. Arg+ or Lys+. They may also occur between ionized organic ligands, such as acetylcholine+ (or example at right: 1cbr), or inorganic ions, such as K+ or Cl-, and amino acid side-chains.

A salt bridge is generally considered to exist when the centers of charge are 4 Å or less apart[1]. The center of charge of the arginine sidechain is the zeta carbon[2]. The energetic significance of such complementary charge pairs is a complex function of the local environment.

Putative salt bridges can be displayed by FirstGlance in Jmol.

ExamplesExamples

Ultraviolet-B receptorUltraviolet-B receptor

UVR8 is an ultraviolet-B receptor in plants such as Arabidopsis. It is a homodimer that, upon irradiation, dissociates into a monomer involved in transcriptional activation of UV protective proteins[3]. Unexpectedly, high ionic strength was found to dissociate the dimer. The homodimer 4dnw contains many salt bridges and cation-pi interactions at the interface.

ReferencesReferences

  1. Jeffrey, George A., An introduction to hydrogen bonding, Oxford University Press, 1997. Page 192.
  2. Gallivan JP, Dougherty DA. Cation-pi interactions in structural biology. Proc Natl Acad Sci U S A. 1999 Aug 17;96(17):9459-64. PMID:10449714
  3. Wu D, Hu Q, Yan Z, Chen W, Yan C, Huang X, Zhang J, Yang P, Deng H, Wang J, Deng X, Shi Y. Structural basis of ultraviolet-B perception by UVR8. Nature. 2012 Feb 29;484(7393):214-9. doi: 10.1038/nature10931. PMID:22388820 doi:10.1038/nature10931

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