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Abstract The use of fluorine has become well established in the analysis of protein structure and function, e.g. in tools such as 19 F NMR spectroscopy. The application of the unique electronic properties of this element for the structural and chemical modification of peptides and proteins emerged as a promising approach. However, the influences of amino acid fluorination on side‐chain interactions in proteins are still controversially discussed. The systematic investigation of the interaction properties of fluoroalkyl groups in a native polypeptide environment broadens the scope of fluorinated amino acids to the rational design of structural motifs and protein interfaces. (© Wiley‐VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2005)
Jäckel et al. (Fri,) studied this question.