1myl
From Proteopedia
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'''SUBSTITUTING HYDROPHOBIC RESIDUES FOR A BURIED SALT BRIDGE ENHANCES PROTEIN STABILITY BUT DOES NOT REDUCE CONFORMATIONAL SPECIFICITY''' | '''SUBSTITUTING HYDROPHOBIC RESIDUES FOR A BURIED SALT BRIDGE ENHANCES PROTEIN STABILITY BUT DOES NOT REDUCE CONFORMATIONAL SPECIFICITY''' | ||
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[[Category: Schildbach, J F.]] | [[Category: Schildbach, J F.]] | ||
[[Category: Waldburger, C D.]] | [[Category: Waldburger, C D.]] | ||
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Revision as of 22:52, 2 May 2008
SUBSTITUTING HYDROPHOBIC RESIDUES FOR A BURIED SALT BRIDGE ENHANCES PROTEIN STABILITY BUT DOES NOT REDUCE CONFORMATIONAL SPECIFICITY
Overview
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.
About this Structure
1MYL is a Single protein structure of sequence from Enterobacteria phage p22. Full crystallographic information is available from OCA.
Reference
Are buried salt bridges important for protein stability and conformational specificity?, Waldburger CD, Schildbach JF, Sauer RT, Nat Struct Biol. 1995 Feb;2(2):122-8. PMID:7749916 Page seeded by OCA on Sat May 3 01:52:27 2008
