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

Study Summary

Number of data points 21
Proteins Repressor protein cI ; Repressor protein cI
Unique complexes 6
Assays/Quantities/Protocols Experimental Assay: ddG ; Experimental Assay: dHcal ; Experimental Assay: Tm ; Derived Quantity: dTm
Libraries Mutations for sequence STKKKPLTQEQLEDARRLKAIYEKKKNELGLSQESVADKMGMGQSGVGALFNGINALNAYNAALLAKILKVSVEEFSPSIAREIYEMYEAVS

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Repressor protein cI P03034 RPC1_LAMBD