While most a-helical residues exhibited rapid dephasing due to relatively short interhelical distances, some residues displayed slower dephasing times, indicative of extended backbone conformations, illustrated in Fig. 9. Using TALOS + torsion angle predictions [108] and the 15N-BARE data as restraints [109], structure calculations of CA were run with Xplor-NIH [110] and revealed that the 310-helix near the CTD–NTD linker is in a more extended conformation than indicated in solution NMR studies, and also distinguished differences in the loops between H3 and H4 and H10 and H11