Cungen Zhang. NOESY experiment. noesy 90. at, t2. mix

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Transcription:

NOESY experiment 90 noesy 90 90 Cungen Zhang at, t2 d1 t1 mix Nuclear Overhauser Effect SpectroscopY is a 2D spectroscopy method whose aim is to identify spins undergoing cross-relaxation and to measure the cross-relaxation rates. Most commonly, NOESY is used as a homonuclear 1H technique. In NOESY, direct dipolar couplings provide the primary means of cross-relaxation, and so spins undergoing crossrelaxation are those which are close to one another in space. Thus, the cross peaks of a NOESY spectrum indicates which 1H s are close to which other 1H s in space. This can be distinguished from COSY, for example, which relies on J-coupling to provide spinspin correlation, and whose cross peaks indicate which 1H s are close to which other 1H s through the bonds of the molecule. The basic NOESY sequence consists of three 90 pulses. The first pulse creates transverse spin magnetization. This precesses during the evolution time t1, which is incremented during the course of the 2D experiment providing chemical shift information in the F1 domain. The second pulse transmits some of the magnetization to the Z axis and during the following mixing period, the non-equilibria Z component will exchange magnetization through relaxation (dipole-dipole mechanism). This exchange of magnetization is known as NOE (Nuclear Overhauser Effect). Thus, the basic idea is to produce an initial situation for the mixing period τ m (the time during which cross relaxation occurs) where the longitudinal polarization of each spin is labelled by its resonance frequency. The longitudinal magnetization is allowed to relax during the mixing time τ m. Note that, for the basic NOESY experiment, τ m is kept constant throughout the 2D experiment. The third pulse creates transverse magnetization from the remaining longitudinal magnetization. Acquisition begins immediately following the third pulse, and the transverse magnetization is observed as a function of the time t2. The NOESY spectrum is generated by a 2D Fourier transform with respect to t1 and t2. Axial peaks, which originate from magnetization that has relaxed during τ m, can be removed by the appropriate phase cycling.

NOESY is one of the most useful techniques as it allows to correlate nuclei through space (distance smaller than 5Å). By measuring cross peak intensity, distance information can be extracted. 2D NOESY Experiment 1. Run a 1D spectrum place two cursors at both sides ~1 ppm away from the peak.. Move sweep width. Too short sw would cause phase distortion. This would cause streaks in the contour plot as shown below. 2. mf(1,2) jexp2.

3. NOESY. (for lower case noesy, hsgt is off). 4. dg. 5. dps. 6. d1=0.5 ( =2~4T1, T1=200 ms), Too small d1 will cause very bad t1 noise. 7. np=2048, this will set up at; at=np/(2sw)=0.139. 8. ni=200, this is the number of points in t1. The default number set by macro should be ok. Keep in mind that sw1/(2ni) should be 6~12 Hz/pt, the digital resolution on F1. 9. mix=0.2, set it close to T1(200 ms) should provide maximized crosspeaks. For high MW, mix=0.3 should be ok. mix is the time period (in seconds) during which magnetization is transferred from one 1 H to another 1 H. mix must be long

enough to transfer magnetization between spins to "build up" the NOESY cross peak intensity between the two spins. If mix is too long though, the magnetization transferred to the second 1 H will "diffuse" to additional spins, decreasing the NOESY cross-peak intensity between the two spins and creating new cross peaks between spins that are farther apart than 5A. Typical values for mix range from 0.2 to 1.2 seconds depending upon the sample's molecular weight; 0.8 is generally a good starting point. 10. Optimize gain. 11. To optimize baseline flatness for the sw, sw1 you set up, please do the following to optimize alfa and rof2. acquire spectra with ni = 2, and phase carefully run calfa which uses the lp value from the phasing reacquire the ni = 2 data and rephase; you should get a good phase with lp=0; if you do not, rerun calfa and require again if the baseline still has some curvature (either convex or concave), then you might want to: note the values of rof2 and alfa keeping the sum rof2+alfa constant, change rof2 and alfa. Do array on both (see metal protein NMR) reacquire and note the effect of the change with rof2 and alfa; one direction should move the baseline towards convex, the other towards concave; some combination should give optimal baseline flatness write down the values of sw rof2 and alfa; these should always work for this sw as a minimum, estimate T1 using inversion-recovery null method to provide setting for d1 12. go. 13. save your original FID. svf( cungen ). 14. Click at MainMenu, AutoProcess, you will see the following spectrum.

15. wft(1). 16. wti. phase it as you did on a normal 1D.

adjust gf to the end of FID. 17. wft1da. 18. Click on trace. 19. Choose one trace. 20. ds. 21. wti. 22.adjust gf1 to the end of FID.

22. pmode= full wft2da. 23. point the mouse at the right upper peak, ds.

phase the the spectrum. 24. dconi. Point the mouse at the lower left peak, ds. 25. click at the right of the spectrum no adjustment please to finish the zero-order phase. This will keep the value you got from the first spectrum. 26. Phase the left peak. Adjust the baseline only. This is the first-order phase. 27. dconi. 28. trace= f2 dconi. Phase the 2D on F2 as you did on F1. 29. dconi.

30. 31. To show 1D on both sides, dconi wc=130 wc2=130 then click ManMenu Plot Proj Hproj(max){adjust vs} Vproj(max). 32. Click autoplot to print out the 2D spectrum. You have successfully done the 2D.