Structure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein design


Abstract

Six helix surface positions of protein G (Gβ1) were redesigned using a computational protein design algorithm, resulting in the five fold mutant Gβ1m2. Gβ1m2 is well folded with a circular dichroism spectrum nearly identical to that of Gβ1, and a melting temperature of 91°C, ~6°C higher than that of Gβ1. The crystal structure of Gβ1m2 was solved to 2.0 Å resolution by molecular replacement. The absence of hydrogen bond or salt bridge interactions between the designed residues in Gβ1m2 suggests that the increased stability of Gβ1m2 is due to increased helix propensity and more favorable helix dipole interactions.

Submission Details

ID: BFPLXTrP3

Submitter: Marie Ary

Submission Date: March 1, 2017, 6:23 p.m.

Version: 1

Publication Details
Strop P;Marinescu AM;Mayo SL,Protein Sci (2000) Structure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein design. PMID:10933505
Additional Information

Study Summary

Number of data points 1
Proteins Protein Gβ1
Unique complexes 1
Assays/Quantities/Protocols Experimental Assay: Tm pH5.0
Libraries CPD of 6 helix surface positions (22,24,28,32,35,36)

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)