Solution NMR structure of fold-U Nomur; de novo designed protein with an asymmetric all-alpha topology

Chemical shift reference of 1H was based on the proton of water (4.784ppm at 303K) and then those of 15N and 13C were calculated based on their gyro-magnetic ratios.

Design of complicated all-α protein structures.

Solution NMR structure of fold-0 Chantal; de novo designed protein with an asymmetric all-alpha topology

Solution NMR structure of fold-C Rei; de novo designed protein with an asymmetric all-alpha topology

Solution NMR structure of fold-Z Gogy; de novo designed protein with an asymmetric all-alpha topology

Solution NMR structure of fold-K Mussoc; de novo designed protein with an asymmetric all-alpha topology

0.8 mM [U-100% 13C; U-100% 15N] foldU5, 1.06 mM potassium phosphate, 2.97 mM sodium phosphate, 155.2 mM sodium chloride, 10 uM EDTA, 0.02 % sodium azide, 0.16 % w/w protease inhibitor complete cocktail, 95% H2O/5% D2O

0.4 mM [U-100% 13C; U-100% 15N] foldU5, 1.06 mM potassium phosphate, 2.97 mM sodium phosphate, 155.2 mM sodium chloride, 10 mM EDTA, 0.02 % sodium azide, 0.16 % w/w protease inhibitor complete cocktail, 10 mg/mL Pf1 phage, 95% H2O/5% D2O

Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax