Salt bridges: Difference between revisions

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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 can also occur between an inorganic ion, such as K+ or Cl-, and an amino acid side-chain.
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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 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 &Aring; or less apart<ref>Jeffrey, George A., An introduction to hydrogen bonding, Oxford University Press, 1997. Page 192.</ref>. The energetic significance of such complementary charge pairs is a complex function of the local environment.  
A salt bridge is generally considered to exist when the centers of charge are 4 &Aring; or less apart<ref>Jeffrey, George A., An introduction to hydrogen bonding, Oxford University Press, 1997. Page 192.</ref>. The energetic significance of such complementary charge pairs is a complex function of the local environment.  

Revision as of 21:14, 3 February 2010

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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 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 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.

ReferencesReferences

  1. Jeffrey, George A., An introduction to hydrogen bonding, Oxford University Press, 1997. Page 192.

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