Identifying determinants of folding and activity for a protein of unknown structure.


Abstract

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

Submission Details

ID: FgSDagQW3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:16 p.m.

Version: 1

Publication Details
Bowie JU;Sauer RT,Proc. Natl. Acad. Sci. U.S.A. (1989) Identifying determinants of folding and activity for a protein of unknown structure. PMID:2928323
Additional Information

Sequence Assay Result Units