Nuclear magnetic resonance hydrogen exchange

Mueller, G.A., Smith, A.M., Chapman, M.D., Rule, G.S., and Benjamin, D.C. 2001. Hydrogen exchange nuclear magnetic resonance spectroscopy mapping of antibody epitopes on the house dust mite allergen Derp 2. J Biol Chem 276(12) 9359-9365. 

Physical Chemical Characterization. Thiamine, its derivatives, and its degradation products have been fully characterized by spectroscopic methods (9,10). The ultraviolet spectmm of thiamine shows pH-dependent maxima (11). H, and nuclear magnetic resonance spectra show protonation occurs at the 1-nitrogen, and not the 4-amino position (12—14). The H spectmm in D2O shows no resonance for the thiazole 2-hydrogen, as this is acidic and readily exchanged via formation of the thiazole yUd (13) an important intermediate in the biochemical functions of thiamine. Recent work has revised the piC values for the two ionization reactions to 4.8 and 18 respectively (9,10,15). The mass spectmm of thiamine hydrochloride shows no molecular ion under standard electron impact ionization conditions, but fast atom bombardment and chemical ionization allow observation of both an intense peak for the patent cation and its major fragmentation ion, the pyrimidinylmethyl cation (16). 

Kamel AM, Zandi KS, Massefski WW. 2003. Identification of the degradation product of ezlopitant, a non-peptidic substance P antagonist receptor, by hydrogen deuterium exchange, electrospray ionization tandem mass spectrometry (ESI/MS/MM) and nuclear magnetic resonance (NMR) spectroscopy. J Pharm Biomed Anal 31 1211. 

Nuclear magnetic resonance measurements show that the hydrogen atoms of NH3 rapidly exchange with those of water by the process... 

The nuclear magnetic resonance (NMR) spectrum (Fig. 2) was obtained by preparing a saturated solution of meperidine hydrochloride, U.S.P. (Wyeth Lot No. F-665901) in deutero chloroform containing tetramethylsilane as internal reference. The only exchangeable proton is the hydrogen associated with HC1. The NMR proton spectral assignments are given in Table II. 

Historically, hydrogen exchange experiments (i.e., the replacement of one isotope of hydrogen bound to an O, N, or S atom in the protein interior by another isotope from the solvent water) provided some of the earliest evidence for the existence of conformational fluctuations in proteins. More recently, a wide range of experimental methods (such as fluorescence quenching and depolarization, nuclear magnetic resonance relaxation, infrared and Raman spectroscopy, and X-ray and inelastic neutron scattering) have been used to study the motions in proteins. However, it is primarily the application of theoretical methods, particularly molecular dynamics simulations, that have... 

Hydrogen Exchange Measured by Nuclear Magnetic Resonance (NMR) Spectroscopy... 

---