Stabilization of lambda repressor against thermal denaturation by site-directed Gly----Ala changes in alpha-helix 3.


Abstract

Oligonucleotide-directed mutagenesis has been used to replace alpha-helical glycines in the N-terminal domain of lambda repressor with alanines. Since alanine is a significantly better helix-forming residue than glycine, these changes were predicted to have a stabilizing effect. We show that the Gly46----Ala substitution, the Gly48----Ala substitution, and the double substitution increase the melting temperature of the N-terminal domain by 3-6 degrees. Study holds ProTherm entries: 790, 791, 792, 793, 2273, 2274, 13412, 13413, 13414, 13985, 13986 Extra Details: alpha helix; lambda repressor; stabilizing effect;,melting temperature

Submission Details

ID: AdDkHwEm

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:15 p.m.

Version: 1

Publication Details
Hecht MH;Sturtevant JM;Sauer RT,Proteins (1986) Stabilization of lambda repressor against thermal denaturation by site-directed Gly----Ala changes in alpha-helix 3. PMID:3449850
Additional Information

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