Engineering and characterization of a pH‐sensitive homodimeric antiparallel coiled coil 

Hand holding anitparallel coiled coil protein

Although there are numerous reports of parallel coiled coil proteins with pH sensitive folding, there are relatively few examples of antiparallel systems. Beginning with a mutated fragment of Bcr‐Abl, an oncoprotein implicated in human leukemia, Schneider and co‐workers use a structure‐based engineering approach to generate a new pH sensitive homodimeric anti‐parallel two‐stranded coiled coil. The protein is stable under acidic solution conditions but unfolds under basic conditions with two state behavior that is governed by a glutamic acid within its hydrophobic core. When deprotonated, the glutamate destabilizes the folded state via charge repulsion with an existing Glu in the core. Responsive antiparallel coiled coils should find use in the preparation of smart self‐assembled materials.

Lab/Branch/Program: 
Chemical Biology Laboratory
Citation: 

Engineering and characterization of a pH‐sensitive homodimeric antiparallel coiled coil by Radhika P. Nagarkar  Galit Fichman  Joel P. Schneider in Peptide Science, 2020112, e24180

Published Date: 
August, 2020