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Salt bridges

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

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 SO4=, 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.

Proteins from thermophiles have more salt bridges than do proteins from mesophiles[3][4]. These additional salt bridges contribute to stability, resisting denaturation by high temperature[5].

Contents

Examples

Ultraviolet-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[6]. Unexpectedly, high ionic strength was found to dissociate the dimer. The homodimer 4dnw contains many salt bridges and cation-pi interactions at the interface. More.

Visualization

Putative salt bridges can be displayed by FirstGlance in Jmol.


References

  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. Das R, Gerstein M. The stability of thermophilic proteins: a study based on comprehensive genome comparison. Funct Integr Genomics. 2000 May;1(1):76-88. PMID:11793224 doi:10.1007/s101420000003
  4. Kumar S, Nussinov R. How do thermophilic proteins deal with heat? Cell Mol Life Sci. 2001 Aug;58(9):1216-33. PMID:11577980
  5. Chan CH, Yu TH, Wong KB. Stabilizing salt-bridge enhances protein thermostability by reducing the heat capacity change of unfolding. PLoS One. 2011;6(6):e21624. Epub 2011 Jun 24. PMID:21720566 doi:10.1371/journal.pone.0021624
  6. 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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