Abstract
AbstractThe use of fluorine has become well established in the analysis of protein structure and function, e.g. in tools such as 19F 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)
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