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. Author manuscript; available in PMC: 2011 Mar 1.
Published in final edited form as: J Struct Biol. 2009 Sep 30;169(3):349–359. doi: 10.1016/j.jsb.2009.09.011

Table 2.

Mutational analysis of VEK-30 variants binding to K2Pg by surface plasmon resonance and circular dichroism

Peptide kona koff KD Apo-helicityb Maximum helicityc
M−1 s−1 s−1 nM % %
VEK-30 4.54×105 2.93×10−2 65 34 74
VEK-30[D7A] 1.26×105 5.61×10−2 446 29 58
VEK-30[D7N] 3.62×104 7.04×10−2 1940 18 23
VEK-30[D7N/E9Q] 5.04×104 8.60×10−2 1710 12 26
VEK-30[D7A/E9A] 2.61×105 9.67×10−2 371 19 52
a

The association rate constant (kon) and dissociation rate constant (koff) were obtained by SPR and apparent equilibrium dissociation constants (KD) were calculated from the ratio of koff/kon.

b

% α-helix in absence of K2Pg.

c

% maximal attainable a-helix after titration with K2Pg.