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. Author manuscript; available in PMC: 2008 Aug 17.
Published in final edited form as: Biochemistry. 2006 Jun 20;45(24):7586–7597. doi: 10.1021/bi0603928

Figure 5.

Figure 5

Proposed H-bonding Interactions Between Backbone Amide Protons and Carboxyl Side-chains: DFDGAM-NH2 = Peptide 3, DFDGAMPGVLRF-NH2 = Peptide 2, DFDGEMPGVLRF-NH2 = Peptide 4, SGSGAMPGVLRF-NH2 = Peptide 5, EMPGVLRF-NH2 = Peptide 2. Each H-bond acceptor residue is color coded to match the arrows leading from it to its H-bond donors. The arrow widths are proportional to the relative extent to which that particular interaction affects the chemical shift of the amide proton at the point end of the arrow. The bar plots show the temperature coefficient of the backbone amide proton resonances