Placement of 19F into the center of GB1: effects on structure and stability

Abstract

5F-Trp-substituted immunoglobulin binding domain B1 of streptococcal protein G (GB1) was carried out by nuclear magnetic resonance and circular dichroism spectroscopy. A single fluorine reporter atom was positioned at the center of the three-dimensional structure, uniquely poised to be exploited for studying interior properties of this protein. We demonstrate that the introduction of 5F-Trp does not affect the global and local architecture of GB1 and has no influence on the thermodynamic stability. The favorable properties of the fluorinated GB1 render this molecule a desirable model system for the development of spectroscopic methodology and theoretical calculations.

Submission Details

ID: 2BHxdak5

Submitter: Marie Ary

Submission Date: July 31, 2017, 11:46 a.m.

Version: 1

Publication Details
Campos-Olivas R;Aziz R;Helms GL;Evans JN;Gronenborn AM,FEBS Lett (2002) Placement of 19F into the center of GB1: effects on structure and stability. PMID:12062409
Additional Information

Study Summary

Number of data points 2
Proteins Protein Gβ1
Unique complexes 2
Assays/Quantities/Protocols Experimental Assay: Tm pH5.5
Libraries Stability of WT and Y3F;Y45F mutant

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)