Fluoroproline Flip-Flop: Regiochemical Reversal of a Stereoelectronic Effect on Peptide and Protein Structures

摘要

The de novo design of protein structure relies on the ability to uniquely define a polypeptide chain conformation through introduction of specific stabilizing interactions into the amino acid sequence, which act cooperatively to overcome the loss of conformational entropy associated with the protein folding process. Within this concept, the stereoelectronic effect has recently emerged as a means to restrict the local chain conformation of polypeptide sequences and to modulate the thermodynamic stability of secondary and supersecondarystructural elements.