Effect of single amino acid replacements on the thermal stability of the NH2-terminal domain of phage lambda repressor.


Abstract

The thermal stabilities of mutant phage lambda repressors that have single amino acid replacements in the NH2-terminal domain have been studied by means of circular dichroism and differential scanning calorimetry. The variations in stability determined by these physical methods correlate with the resistance to proteolysis at various temperatures and can be compared with the temperature-sensitive activity of the mutants in vivo. In general, mutant proteins bearing solvent-exposed substitutions have thermal stabilities identical to wild type, whereas buried substitutions reduce stability. In one case, a single amino acid replacement increases the thermal stability of the repressor. Study holds ProTherm entries: 794, 795, 796, 797, 798, 799, 800, 801, 13415, 13416, 13417, 13418, 13419, 13420, 13421 Extra Details: NaN3(1 mM) was added in the experiment phage lambda receptor; amino acid replacement; thermal stability;,activity; calorimetry

Submission Details

ID: reen8gfV

Submitter: Connie Wang

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

Version: 1

Publication Details
Hecht MH;Sturtevant JM;Sauer RT,Proc. Natl. Acad. Sci. U.S.A. (1984) Effect of single amino acid replacements on the thermal stability of the NH2-terminal domain of phage lambda repressor. PMID:6237363
Additional Information

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