Are buried salt bridges important for protein stability and conformational specificity? - PubMed

Are buried salt bridges important for protein stability and conformational specificity?

C D Waldburger et al. Nat Struct Biol. 1995 Feb.

Abstract

The side chains of Arg 31, Glu 36 and Arg 40 in Arc repressor form a buried salt-bridge triad. The entire salt-bridge network can be replaced by hydrophobic residues in combinatorial randomization experiments resulting in active mutants that are significantly more stable than wild type. The crystal structure of one mutant reveals that the mutant side chains pack against each other in an otherwise wild-type fold. Thus, simple hydrophobic interactions provide more stabilizing energy than the buried salt bridge and confer comparable conformational specificity.

Comment in

• Can proteins be turned inside-out?

  Matthews BW. Matthews BW. Nat Struct Biol. 1995 Feb;2(2):85-6. doi: 10.1038/nsb0295-85. Nat Struct Biol. 1995. PMID: 7749923 No abstract available.

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