There are two other ways that come to mind for establishing hydrogen bondedness and h-bond strength, though they don't identify H-bonded partners.

First is measuring H/D fractionation factors. factors. Without going into great detail, one integrates the putatively H-bonded hydrogen in a series of H2O/D2O mixtures. If the hydrogen is only h-bonded with solvent, it will integrate to 0.5 in a 50/50 H2O/D2O mixture.

If the H-bond is strong, the hydrogen will be selectively enriched because of differential zero point energies. I haven't kept up on this literature, but you can check out the following references on the subject. It was a hot subject in Madison for awhile. (1) awhile.

1. Lin, J.; Frey, P. A. Journal of the American Chemical Society 2000, 122, 11258-11259. (2) 11258-11259.
2. Lin, J.; Westler, W. M.; Cleland, W. W.; Markley, J. L.; Frey, P. A. Proceedings of the National Academy of Sciences of the United States of America 1998, 95, 14664-8. (3) 14664-8.
3. LiWang, A. C.; Bax, A. Journal of the American Chemical Society 1996, 118, 12864-12865. (4) 12864-12865.
4. Loh, S. N.; Markley, J. L. Biochemistry 1994, 33, 1029-1036.

Second, there's this old reference that you may find particularly useful: (1) useful:

1. Gunnarsson, G.; Wennerstrom, H.; Egan, W.; Forsen, S. Chemical Physics Letters 1976, 38, 96-9. 96-9.

The main message is that if you compare 1H and 2H spectra of hydrogen-bonded systems, the chemical shifts of the signals will differ in proportion to their h-bond strength. In principle, if you took 1D 1H and 2H spectra of your peptide in 50/50 H/D2O, you'd observe slight differences between the frequencies of the same residue's amide "H" depending on whether it was 1H or 2H. Never tried it myself, but thought it might be useful.

There are two other ways that come to mind for establishing hydrogen bondedness and h-bond strength, though they don't identify H-bonded partners.

First is measuring H/D fractionation factors. Without going into great detail, one integrates the putatively H-bonded hydrogen in a series of H2O/D2O mixtures. If the hydrogen is only h-bonded with solvent, it will integrate to 0.5 in a 50/50 H2O/D2O mixture.

If the H-bond is strong, the hydrogen will be selectively enriched because of differential zero point energies. I haven't kept up on this literature, but you can check out the following references on the subject. It was a hot subject in Madison for awhile.

1. Lin, J.; Frey, P. A. Journal of the American Chemical Society 2000, 122, 11258-11259.
2. Lin, J.; Westler, W. M.; Cleland, W. W.; Markley, J. L.; Frey, P. A. Proceedings of the National Academy of Sciences of the United States of America 1998, 95, 14664-8.
3. LiWang, A. C.; Bax, A. Journal of the American Chemical Society 1996, 118, 12864-12865.
4. Loh, S. N.; Markley, J. L. Biochemistry 1994, 33, 1029-1036.

Second, there's this old reference that you may find particularly useful:

1. Gunnarsson, G.; Wennerstrom, H.; Egan, W.; Forsen, S. Chemical Physics Letters 1976, 38, 96-9.

The main message is that if you compare 1H and 2H 2H spectra of hydrogen-bonded systems, the chemical shifts of the signals will differ differ in proportion to their h-bond strength. In principle, if you took 1D 1H and 2H spectra of your peptide in 50/50 H/D2O, you'd observe slight differences between the frequencies of the same residue's amide "H" depending on whether it was 1H or 2H. Never tried it myself, but thought it might be useful.