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. Author manuscript; available in PMC: 2014 Jun 21.
Published in final edited form as: Phys Chem Chem Phys. 2013 Mar 20;15(23):8916–8928. doi: 10.1039/c3cp00063j

Fig 7.

Fig 7

Correlation between number of hydrogen bonds and presence of salt bridges. The higher number of hydrogen bonds formed by the back bone of the R2/wt (a) is associated to the presence of the salt bridge K280-D283 (b). On the other hand, the mutant R2/ΔK280 forms a lower number of hydrogen bonds (c) as a consequence of the lack of a side chain hydrogen bond N279-D283(d). Data have been collected for the peptides in solution with z/n=+2/1 for R2/wt and z/n=+1/1 for R2/ΔK280. See also Figure S1 and S2 for how theoretical CCSs have been computed.