Solvation and Hydrogen Bonding in Alanine- and Glycine-Containing Dipeptides Probed Using Solution- and Solid-State NMR Spectroscopy Export

@article{citeulike:4896239, abstract = {PMID: 19537718 The NMR chemical shift is a sensitive reporter of peptide secondary structure and its solvation environment, and it is potentially rich with information about both backbone dihedral angles and hydrogen bonding. We report results from solution- and solid-state 13C and 15N NMR studies of four zwitterionic model dipeptides, l-alanyl-l-alanine, l-alanyl-glycine, glycyl-l-alanine, and glycyl-glycine, in which we attempt to isolate structural and environmental contributions to the chemical shift. We have mapped hydrogen-bonding patterns in the crystalline states of these dipeptides using the published crystal structures and correlated them with 13C and 15N magic angle spinning chemical shift data. To aid in the interpretation of the solvated chemical shifts, we performed ab initio quantum chemical calculations to determine the low-energy conformers and their chemical shifts. Assuming low energy barriers to interconversion between thermally accessible conformers, we compare the Boltzmann-averaged chemical shifts with the experimentally determined solvated-state shifts. The results allow us to correlate the observed differences in chemical shifts between the crystalline and solvated states to changes in conformation and hydrogen bonding that occur upon solvation.}, author = {Bhate, Manasi P. and Woodard, Jaie C. and Mehta, Manish A.}, citeulike-article-id = {4896239}, citeulike-linkout-0 = {http://dx.doi.org/10.1021/ja902917s}, citeulike-linkout-1 = {http://pubs.acs.org/doi/abs/10.1021/ja902917s}, doi = {10.1021/ja902917s}, journal = {Journal of the American Chemical Society}, keywords = {ala, alanine, dipeptide, gly, glycine, hydrogen-bonds, solvation}, month = {July}, number = {27}, pages = {9579--9589}, posted-at = {2009-07-11 20:34:08}, priority = {2}, title = {Solvation and Hydrogen Bonding in Alanine- and Glycine-Containing Dipeptides Probed Using Solution- and Solid-State NMR Spectroscopy}, url = {http://dx.doi.org/10.1021/ja902917s}, volume = {131}, year = {2009} }

TY - JOUR ID - citeulike:4896239 L3 - citeulike-article-id:4896239 N2 - PMID: 19537718 The NMR chemical shift is a sensitive reporter of peptide secondary structure and its solvation environment, and it is potentially rich with information about both backbone dihedral angles and hydrogen bonding. We report results from solution- and solid-state 13C and 15N NMR studies of four zwitterionic model dipeptides, l-alanyl-l-alanine, l-alanyl-glycine, glycyl-l-alanine, and glycyl-glycine, in which we attempt to isolate structural and environmental contributions to the chemical shift. We have mapped hydrogen-bonding patterns in the crystalline states of these dipeptides using the published crystal structures and correlated them with 13C and 15N magic angle spinning chemical shift data. To aid in the interpretation of the solvated chemical shifts, we performed ab initio quantum chemical calculations to determine the low-energy conformers and their chemical shifts. Assuming low energy barriers to interconversion between thermally accessible conformers, we compare the Boltzmann-averaged chemical shifts with the experimentally determined solvated-state shifts. The results allow us to correlate the observed differences in chemical shifts between the crystalline and solvated states to changes in conformation and hydrogen bonding that occur upon solvation. IS - 27 JF - Journal of the American Chemical Society EP - 9589 TI - Solvation and Hydrogen Bonding in Alanine- and Glycine-Containing Dipeptides Probed Using Solution- and Solid-State NMR Spectroscopy VL - 131 SP - 9579 KW - ala KW - alanine KW - dipeptide KW - gly KW - glycine KW - hydrogen-bonds KW - solvation AU - Bhate, Manasi AU - Woodard, Jaie AU - Mehta, Manish PY - 2009/07/15/ UR - http://dx.doi.org/10.1021/ja902917s ER -