Four-helix bundle cavitein reveals middle leucine as linchpin.

Abstract

A template-assembled de novo four-helix bundle is used to examine the hydrophobic effect within the bundle interior. Leu to Ala variants of the basis sequence GG-EELLKKLEELLKKG were characterized by GuHCl denaturation, NMR dispersion, and N-H/D exchange experiments. The results show that the middle leucine (L7) is imperative in maintaining bundle stability. The average leucine was found to contribute 1.8 kcal mol(-1) toward stability, whereas the middle leucines contribute 2.7 kcal mol(-1) each. Substituting alanine into the middle position (7) constitutes a striking 95% reduction of the overall cavitein stability.

Cite this paper

@article{Freeman2007FourhelixBC, title={Four-helix bundle cavitein reveals middle leucine as linchpin.}, author={Jon O Freeman and Diana Wallhorn and John C. Sherman}, journal={Biopolymers}, year={2007}, volume={88 5}, pages={725-32} }