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Placement of 19 F into the center of GB1: effects on structure and stability
Author(s) -
Campos-Olivas Ramón,
Aziz Rehan,
Helms Gregory L,
Evans Jeremy N.S,
Gronenborn Angela M
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02577-2
Subject(s) - center (category theory) , chemistry , stability (learning theory) , crystallography , computer science , machine learning
A structural and thermodynamic characterization of 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.