Journal
FEBS LETTERS
Volume 517, Issue 1-3, Pages 55-60Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(02)02577-2
Keywords
immunoglobulin G binding domain B1 of; streptococcal protein G; fluorine substitution; protein structure; nuclear magnetic resonance
Funding
- NCRR NIH HHS [RR12948, RR0631401] Funding Source: Medline
- NIGMS NIH HHS [R01 GM43215] Funding Source: Medline
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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. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
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