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. 2005 May;79(10):6134–6141. doi: 10.1128/JVI.79.10.6134-6141.2005

FIG. 6.

FIG. 6.

Temperature dependence of aliphatic proton NMR resonances in wild-type and mutant gH peptides. (A) 1D 1H NMR spectra of wild-type (WT) gH peptide recorded from 2°C (bottom) to 45°C (top). The red lines indicate a significant change in chemical shift with temperature. (B) 1D 1H NMR spectra of gH PA mutant peptide recorded from 2 to 40°C. The red lines indicate little to no change in chemical shift with temperature. (C) Temperature profiles of three individual resonances (Arg4, Pro8, and Phe10, indicated in the single-letter amino acid code) of the wild-type gH peptide indicating cooperative changes with temperature.