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. 2015 Oct 7;89(24):12467–12479. doi: 10.1128/JVI.01741-15

FIG 6.

FIG 6

Binding stability of C34, SFT, and C34 mutants determined by CD spectroscopy. The α-helicity and thermostability of 6-HBs formed by C34 (A and B) or SFT (C and D) with N36 or its mutants (N36E49K, N36L57R, and N36E49K/L57R) were measured. The Tm value was defined as the midpoint of the thermal unfolding transition. The final concentration of each peptide in PBS is 10 μM. The binding stability of C34 or its mutants (C34N126K, C34E136G, and C34N126K/E136G) with N36 was determined by CD spectroscopy similarly (E and F). The experiments were repeated at least twice, and representative data are shown.