We have generated an extensive genetic map of functionally allowed and/or structurally allowed amino acid substitutions in Arc repressor, a DNA binding protein of unknown structure. Analysis of the allowed substitution patterns identifies residues that are likely to be involved in protein function and identifies side chains that play important structural roles, including residues likely to form the hydrophobic core. The identities of approximately one-third of the residues in Arc repressor are functionally important, about one-half are structurally important, and the remainder are unimportant for either structure or function. The patterns of obligatory hydrophobic positions permit strong predictions of secondary structure. Study holds ProTherm entries: 831, 832, 833, 834, 835, 836, 837, 838, 839, 840, 841, 842, 843, 844, 845, 846, 847, 848, 849 Extra Details: Arc repressor; DNA binding; protein folding;,secondary structure prediction; mutagenesis
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:16 p.m.
|Number of data points||37|
|Proteins||Transcriptional repressor arc ; Transcriptional repressor arc|
|Assays/Quantities/Protocols||Experimental Assay: Tm ; Experimental Assay: ddG_H2O ; Experimental Assay: Cm ; Derived Quantity: dTm|
|Libraries||Mutations for sequence MKGMSKMPQFNLRWPREVLDLVRKVAEENGRSVNSEIYQRVMESFKKEGRIGA|