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Effects of Fluorination on the Folding Kinetics of a Heterodimeric Coiled Coil
Author(s) -
Salwiczek Mario,
Koksch Beate
Publication year - 2009
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200900518
Subject(s) - fluorine , folding (dsp implementation) , coiled coil , kinetics , chemistry , protein folding , biophysics , computational biology , nanotechnology , combinatorial chemistry , biochemistry , materials science , organic chemistry , biology , physics , engineering , quantum mechanics , electrical engineering
The fast and the fluorous: SPR is a powerful method to investigate fast interactions between peptides and proteins. Differences of even one fluorine atom within a side chain can be detected. It is shown that fluorination of a single residue within the hydrophobic core results in a twofold increase in the association rate of a coiled‐coil heterodimer. The observations furthermore reinvigorate the question whether fluorine–fluorine contacts in the unfolded state affect the kinetics of folding.