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
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:15 p.m.
|Number of data points||47|
|Proteins||Repressor protein cI ; Repressor protein cI|
|Assays/Quantities/Protocols||Experimental Assay: activity temp:51.5 C ; Experimental Assay: ddG ; Experimental Assay: activity ; Experimental Assay: dHcal ; Experimental Assay: Tm ; Experimental Assay: dHvH ; Derived Quantity: dTm|
|Libraries||Mutations for sequence STKKKPLTQEQLEDARRLKAIYEKKKNELGLSQESVADKMGMGQSGVGALFNGINALNAYNAALLAKILKVSVEEFSPSIAREIYEMYEAVS|