144 (327) BRUKER BIOSPIN User Manual Version 002
Proton Driven Spin Diffusion (PDSD)
en” relates to recoupling pulses on the X channel, whereas in DARR or RAD the
radio frequency that drives the recoupling is the proton RF.
An important aspect of this experiment is that the mixing time is a simple delay
and no pulse, or only weak rf irradiation (DARR, RAD) is required. Therefore it
can be made very long because no technical or experimental problems can arise.
So the effects even of small dipolar couplings (requiring long spin diffusion times)
can be observed. However the information from this experiment may be ambigu
-
ous, because a rather non-selective transfer (within the proton spin system) is uti-
lized.
Nevertheless, even complex molecules like proteins can be surprisingly well char-
acterized by PDSD experiments with different mixing times. The buildup of cross
peak intensities can be studied and correlated, for instance, to the structure of a
macromolecule in the solid state. The same approach has been used to compare
different states of a protein, i.e. bound to a membrane or free, as can be found in
the recent literature on solid state NMR applied to protein studies.
More elaborate derivatives of PDSD are also known in bio-molecular NMR, where
the unspecific spin diffusion within the proton spin system is filtered through a
double quantum selection (Lange et al.).
References:
1. N.M. Szeverenyi, M.J. Sullivan, and G.E. Maciel, Observation of Spin Exchange by Two-Dimensional
Fourier Transform
13
C Cross Polarization Magic Angle Spinning, J. Magn. Reson. 47, 462-475 (1982).
2. A.F. de Jong, A. P. M. Kentgens, and W. S. Veeman, Two-Dimensional Exchange NMR in Rotating
Solids: a technique to study very slow molecular motions, Chem. Phys. Lett. 109, 4, 337 (1984).
3. Matthias Ernst and Beat H. Meier, „Spin Diffusion“ in Isao Ando and Tetsuo Asakura, Eds., „Solid-
State NMR of Polymers“, pp. 83-122, Elsevier Science Publisher (1998).
4. Matthias Ernst, Arno P.M. Kentgens, and Beat H. Meier, Pure-Phase 2D-Exchange NMR Spectra un-
der MAS, Journal of Magnetic Resonance 138, 66-73 (1999), and references cited therein.
5. K. Takegoshi, Shinji Nakamura and TakehikoTerao,
13
C-
1
H dipolar-assisted rotational resonance in
magic-angle spinning NMR, Chem. Phys. Lett. 2001, 344, 631.
6. F. Castellani, B. van Rossum, A. Diehl, M. Schubert, K. Rehbein and H. Oschkinat, Structure of a pro-
tein determined by solid-state magic-angle-spinning NMR spectroscopy, Nature 420, 98-102 (2002).
7. C.R. Morcombe, V. Gapenenko, R.A. Byrd, and K. W. Zilm, Diluting Abundant Spins by Isotope Edited
Radio Frequency Field Assisted Diffusion, J. Am. Chem. Soc. 126, 7196-7197 (2004).
8. S.G. Zech, A.G. Wand and A.E. McDermott Protein Structure Determination by High-Resolution Solid-
State NMR Spectroscopy: Application to Microcrystalline Ubiquitin, J. Am. Chem. Soc. 127, 8618-
8626 (2005).
9. W. Luo, X. Yao and M. Hong Large Structure Rearrangement of Colicin Ia channel Domain after Mem-
brane Binding from 2D
13
C Spin Diffusion NMR), J. Am. Chem. Soc. 127, 6402-6408 (2005).
10. A.Lange, S. Luca, and M. Baldus, Structural constraints from proton-mediated rare spin correlation
spectroscopy, J. Amer. Chem. Soc., 124, 9704-9705 (2002).
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