Local and macroscopic electrostatic interactions in single α-helices

Emily Baker,1 Gail Bartlett,1 Matt Crump,1 Richard Sessions,2,3 Noah Linden,4 Charl Faul1 and Dek Woolfson1,2,3

Nature Chemical Biology 11, 221 – 228 (2015)

DOI: 10.1038/nchembio.1739


1School of Chemistry 2School of Biochemistry 3BrisSynBio 4School of Mathematics

From Dek: A multidisciplinary team of chemists, biochemists and mathematicians at Bristol have shed light on a controversial 40-year old theory of protein structure.  The research was conducted by Emily Baker and Gail Bartlett working across the groups of Dek Woolfson, Charl Faul and Matt Crump, and in collaboration with Richard Sessions (Biochemistry) and Noah Linden (Mathematics).  Briefly, many papers and textbooks describe how a macroscopic helix dipole can stabilise a-helices in proteins and influence protein folding, structure and function.  Emily’s experiments, and analyses from Gail and Noah, show that the helix macrodipole is in fact vanishingly small compared with other electrostatic interactions that occur more locally in proteins.

A note from Matt: I should also point out that this study was only made possible through the NMR time allocated to us kindly by the Wellcome Trust funded HWB-NMR centre and access to the 900 MHz spectrometer that was essential for resolving the poorly dispersed proton (only!) spectra and taking me back to the good old days of two-dimensional sequential assignment!