Abstract
AbstractSmall changes in the structure of a foldamer may lead to gross changes in conformational preference. We show that the simple insertion or deletion of a single hydrogen bond by changes in pH or by photochemical deprotection is sufficient to refold a helical oligomer, interconverting M and P screw‐sense preference. As a consequence of the switch, information may be transmitted to a remote catalytic site, selectively directing the formation of either of two enantiomeric products by a reaction involving 1,22‐remote intermolecular asymmetric induction.
Highlights
The higher order structure of proteins and peptides is generally remarkably tolerant of modifications of primary structure:[1] the serine proteases, for example, display similar tertiary structures and have near-identical functions across a wide range of organisms, despite variations in their primary sequence of up to 50 %.[2]
It can be argued that the tolerance of variation in protein structure is what allows the process of random mutation and natural selection to proceed.[3]
There are some proteins in which a small conformational change, such as the cis/trans isomerisation of a proline residue, is sufficient to modulate function.[4,5]
Summary
The higher order structure of proteins and peptides is generally remarkably tolerant of modifications of primary structure:[1] the serine proteases, for example, display similar tertiary structures and have near-identical functions across a wide range of organisms, despite variations in their primary sequence of up to 50 %.[2].
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