The equilibrium stabilities of a complete set of single alanine-substitution mutants of the Arc repressor of bacteriophage P22 have been determined by thermal and urea denaturation experiments. Only half the alanine substitutions cause significant changes in stability, with the most deleterious mutations affecting side chains in the hydrophobic core or in salt bridges and hydrogen bonds which are protected from solvent. The five mutations that are most destabilizing affect a cluster of core residues that seem to form a structural foundation for Arc. Study holds ProTherm entries: 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594, 595, 596, 597, 598, 599, 600, 601, 602, 603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 620, 621, 622, 623, 624, 625, 626, 627, 628, 629, 630, 631, 632, 633, 634, 635, 636, 637, 638, 639, 640, 641, 642, 643, 644, 645, 646, 647, 648, 649, 650, 651, 652, 653, 654, 655, 656, 657, 658, 659, 660, 661, 662, 663, 664, 665, 666, 667, 668 Extra Details: additive : EDTA(0.2 mM),Arc st6; carboxy terminal extension with 6 His residues Arc repressor, alanine substitutions; protein stability;,urea denaturation; hydrophobic core; hydrogen bonds
ID: rqShdLt63
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:15 p.m.
Version: 1
Number of data points | 286 |
Proteins | Transcriptional repressor arc ; Transcriptional repressor arc |
Unique complexes | 47 |
Assays/Quantities/Protocols | Experimental Assay: Tm ; Experimental Assay: dHvH ; Experimental Assay: m ; Experimental Assay: dG_H2O ; Derived Quantity: dTm ; Derived Quantity: ddG_H2O |
Libraries | Mutations for sequence MKGMSKMPQFNLRWPREVLDLVRKVAEENGRSVNSEIYQRVMESFKKEGRIGA |
Colors: | D | E | R | H | K | S | T | N | Q | A | V | I | L | M | F | Y | W | C | G | P |
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Percent Identity | Matching Chains | Protein | Accession | Entry Name |
---|---|---|---|---|
100.0 | Transcriptional repressor arc | P03050 | RARC_BPP22 |