Bruker Topspin 3.2 Manual [EBook]

Bruker Topspin 3.2 Manual [EBook]

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Bruker Topspin 3.2 Manual [EBook]Updates on issue can be tracked by clicking on 'Help' at the top right of your iLab account and under Issue Tracking. The facility houses state of the art equipment primarily for solution NMR (Bruker 600, 700, 800 and 900 MHz spectrometers), and a solid state capacity has been added to the Bruker 800 MHz spectrometer. Recently we were able to update the 600 and 700 MHz spectrometers to HDneo consoles and install new cryoprobes with superior sensitivity and capability to do direct 13 C detect as well as 19 F experiments. As a general rule, however, avoid using long names with special characters and spaces. Do I need to rerun it? - There is no need for rerunning such a spectrum and it can be phased correctly using NMR software. This will allow to correct the phase of the peak centred on the vertical red line. Chemical shifts can be recalibrated using NMR software. Take notice of the SR value and use it in 2D spectra, if any. (5) My 2D spectrum failed to run - This usually happens when 1D projections in F2 and F1 dimensions are not available or they are wrongly defined on sample submission. In the example below, the 2D spectrum for the sample in position 31 will run without errors while that for the sample in position 32 will fail: Installed linux headers: sudo apt-get install linux-headers-generic This installed headers for 3.13, whereas the installed version was 3.18, but this does not matter in this case.How do I disable ATM? - See the screenshot below. This means that students and employees at UiB can use the software on their own machine.If you do not find the software, please contact us through UiBhjelp, or on phone 55584700. Remember to enter machine name. New version will come.You can do this on this page. Use your UiB email address to access the academic license. Published in final edited form as: Bio Protoc. 2015 Jul 20; 5(14): e1539.http://forepic.com/_UploadFile/Images/construction-inspection-manual-of-procedures.xml

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Abstract Reconstitution of integral membrane proteins (IMP) in aqueous solutions of detergent micelles has been extensively used in structural biology, using either X-ray crystallography or NMR in solution. Further progress could be achieved by establishing a rational basis for the selection of detergent and buffer conditions, since the stringent bottleneck that slows down the structural biology of IMPs is the preparation of diffracting crystals or concentrated solutions of stable isotope labeled IMPs. Using microcoil equipment for these NMR experiments enables data collection with only micrograms of protein and detergent. This makes serial screens of variable solution conditions viable, enabling the optimization of parameters such as the detergent concentration, sample temperature, pH and the composition of the buffer. Materials and Reagents Studies of IMPs. High average peak intensity and uniform distribution of peak intensities Analysis of the peak line shapes to support the interpretation of the peak intensity measurements. Determine the translational diffusion coefficient, D t, using the 1 H-TRO-STE experiment. Determine the rotational diffusion coefficient, D r, using the TRACT experiment. Optimize sample conditions towards small R h values, which favors the recording of high-quality NMR data. Data analysis Processing and analysis of NMR datasets Process all NMR experiments with the Bruker standard software Topspin. The integrals were fitted to a mono-exponential decay, using the program XMGRACE ( ). Set the carrier frequency to the water line by minimizing the residual water signal in the Bruker standard pulse sequence zggppr. Typical values for IMP’s reconstituted in detergent micelles are 100 points and 35 ms, respectively. References 1. Bartels C, Xia TH, Billeter M, Guntert P, Wuthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. Susac L, Horst R, Wuthrich K.http://cdosfera.rinethost.ru/userfiles/construction-inspection-manual-download.xml Solution-NMR characterization of outer-membrane protein A from E. coli in lipid bilayer nanodiscs and detergent micelles. Zhang Q, Horst R, Geralt M, Ma X, Hong WX, Finn MG, Stevens RC, Wuthrich K. Microscale NMR screening of new detergents for membrane protein structural biology. You can modify the parameters and saveBruker predefined parameterPROTON all ), set the pulse lengths and power levels by xau gpro If you are using the Bruker predefined parameterThe emphasis is on the spectroscopicThese experiments usually require lessThey Do So if you acquire the corresponding 1D experiments. Typical researchers come from a wide range of disciplines such as chemistry, geology, biochemistry, biology, pharmacy, or engineering. The technique has many useful applications: A Bruker 5mm TXI probe is usually installed. Therefore, it is not preferable for C-13 observing experiments. A Bruker 5mm BBFO probe is usually installed, tunable to most BB-channel nuclei (including F-19). It runs Automation NMR experiments via IconNMR, with a Bruker 5mm BBO probe. A Bruker 5mm BBO probe is usually installed, tunable to most BB-channel nuclei (excluding F-19). Not what one usually does without having at least learned to fly a small plane. We recommend starting on the autosampler instrument and then graduating to one of the other spectrometers. There is much to learn and it is best done in small bits. Please contact Dr. Jianfeng Zhu to arrange a training session. See and references therein. Also check the information at the CABM website. DSS serves as the direct 1H reference standard in liquid state NMR and other spins are referenced indirectly through gyromagnetic ratios. For substitution method a standard sucrose sample with trace DSS amount can be used. Zero frequency w0 remains constant for a given spectrometer until its lock frequency ( lockfreq on Varian spectrometers) is reset due to B0 drift.https://www.cocreationsmanager.com/blog/drill-press-operator-manual If you are not sure whether w0 has been determined for the current spectrometer setup measure in a 1D 1H spectrum of DSS. It happens because spectrometers are locked by adjusting z0, to make the deuterium line of the solvent match a certain predefined frequency. The chemical shift of water, in particular, has a very strong temperature dependence, which leads to B0 discrepancy. Provide a table or formula for 1H chemical shift of water vs.Typically IN0 is used for the first indirect dimension and IN10 is used for the second. Usually 2 or 4 incremented delays ( D0 and d10 ) used to sample indirect dimensions determined by parameters ND0 and ND10, respectively. See the pulse sequence file for the particular setup. Questions (39) Publications (827) Questions related to TopSpin Lea Fels asked a question related to TopSpin Has anyone seen the following TopSpin error after integration: Unable to read XWIN-NMR manual integration list (int2d). Question 2 answers Feb 27, 2020 I'm integrating all my HSQC spectra in TopSpin 4.0.2 manually with an exported mask. From one day to another TopSpin shows the error message, independent of what data file is opened. Has anyone seen this problem and knows how to fix it? (I uninstalled all software packages and installed them again, this didn't help). Relevant answer Lea Fels Mar 2, 2020 Answer Thank you for your answer. Unfortunately, I did this on Friday, but nothing changed. I fixed it by deleting my antivirus software. Since I use another program, the problem is gone. View 0 Recommendations Tamas Milan Nagy asked a question related to TopSpin How to scale 2D NMR spectra in Topspin 3.0 plot? Question 1 answer Oct 25, 2019 I would like to create stacked figures from 2D NMR plots, however scaling of different spectra is not possible in the plot software. I can't modify the levels by hand, the values simply does not change. Is there any other way to do scaling.https://iprende.com/images/canon-hf-r37-manual.pdf Relevant answer Banchhanidhi Prusti Jan 14, 2020 Answer It is there in topspin, give command plot0 View 0 Recommendations Is it possible to export 2D NMR raw data into ASCII files by using TOPSPIN software. Question 5 answers Nov 21, 2019 Thanks in advance. Relevant answer A researcher Nov 26, 2019 Answer To convert 2D raw data into ascii text you can use the attached au program convser2asc. It will generate a txt file with two colums. The one for a index and the second for the amplitude at this point.I am using TopSpin 3.6 to process it. How can I color code the contour lines in the 2D.What I would do is import the spectra to a vector software program (Adobe Illustrator, affinity designer or similar) and change the colors there. Question 6 answers Sep 30, 2019 I am conducting a seeding experiment via NMR. I want some insight into writing an AU program that raises the temperature to about 37 degC and incubate the sample for 4-5 hours and then returns back to 20 degC, incubates for an hour and then takes a HSQC experiment. I am new to NMR and would be grateful for any helpful insights. I have tried and will continue to try to use the bruker manual, but so far i haven't been lucky yet. Relevant answer Woonghee Lee Oct 1, 2019 Answer You can write python: That will be so much easier than AU. View 8 Recommendations Can I normalize NMR spectra for sample weights in TopSpin. Question 2 answers Sep 25, 2019 This is for quantitative 31P (phosphorous) NMR of lignin. I am using Bruker Topsin 4.0.6 for processing. I am visually comparing multiple NMR spectra in one window by plotting them together. However, the heights of peaks in every spectrum is also dependent on the sample weight, which is not perfectly constant. This small variation in sample weights interferes with the peak intensities. Can I somehow normalize the peaks with sample weight so that I get peak intensities compensated for the individual sample mass. Relevant answer Alfred Ross Sep 30, 2019 Answer Dir Vivek, If RG, NS, P1, SI and all other experimental and processing parameters are identical for the spectra you can use the processing parameter DC to multiply the data with this value.Question 1 answer Jul 24, 2019 I am performing CSA simulation for 31P spectrum using SOLA NMR software package provided by Bruker with TopSpin. Simulation is going very good but it seems there is no option for saving the simulated spectrum as txt file. That will save the simulated spectrum as Bruker processed data (proc). You can save that (do not use proc no 1, as that is where your processed data is). Then you can read your processed spectrum in a new window in Topspin and utilise the au program convbin2asc to create ASCII version of the spectrum. View 0 Recommendations Joseph M. Egan asked a question related to TopSpin What causes 'imperfect' decoupling in HSQC. Question 9 answers Apr 12, 2019 I have a question about a phenomena I've been observing in an edited HSQC. However, when a different pulse (hsqcedetgpsp) is applied (shown in red) the problem reduces considerably, leading me to believe something is not 'set right' for the original pulse. This is not the only time I've seen this problem, although in every case I have observed it, it has been a conformationally locked position on a ring (or fuzed ring). For reference, I've seen it on the 4-position of the Cladinose of Azithromycin (splitting 12Hz), a few methyls of Betulinic Acid (average j values 40Hz). The consistency of these j values leads me to believe it has a lot to do with the j C-H of each set of protons being detected (even though it is not any protons in the area that are allowed to freely rotate. As can be seen above in the Doxycyline problem, the imperfect decoupling was assumed to be from the 02P not being set in the correct spot, and therefore did not cover enough of the collected range.www.goodnutrient.com/userfiles/files/Dodge-Caliber-Owners-Manual-2008.pdf At this time, I've decided to push forward with my solution, but was curious to see what others thought might be going on. I can try to rationalize the difference through intramolecular interactions, but I feel as though this is a bit 'hand-wavy' and would like to know if anyone has any input as to what might be happening. Instead, the negative valley of the multiplets noise are sometimes selected. Thank You Anna Relevant answer Stan Sykora Apr 4, 2019 Answer I see. Yes, it is close to where problems start. I see that you have a very good resolution so going from 64K to 128K (by zero-filling or LP) might help. Also, play with apodization modes. Plain exponential is not very good for this, I would go for Hanning, maybe repeated a couple of times. I am behind the GSD algorithm of Mnova which would handle this OK, but I do not want to appear as a commercial pusher here, I am just the number cruncher. It would use internally some techniques that are probably absent in TopSpin. To start with, try to ZF to 128K and then play a bit with apodization. View 4 Recommendations Naira Mustafa asked a question related to TopSpin How can I normalize NMR spectra by topspin software. Question 2 answers Mar 4, 2019 I run samples on different runs and I want to normalize the spectra as the experiment is quantitative. Relevant answer Naira Mustafa Mar 7, 2019 Answer Thank you Bojidarka B. Ivanova. View 0 Recommendations Gopal Pandit asked a question related to TopSpin How to do the water suppression with proper phase correction for proton NMR in CD3OH in Topspin (600 MHz Brucker). Question 5 answers Feb 18, 2019 how to do the water suppression with proper phase correction for proton NMR in CD3OH. Here I am following presaturation method for water suppression.My sample is a Peptide. I am getting huge negative phase of water after performing the experiment with the pulse program zgpr. Need Proper solution to overcome this problem. Relevant answer Jani Rahkila Feb 20, 2019 Answer Using water suppression is perfectly fine (and sometimes absolutely necessary), but you might lose some signals close to the water peak as well. If you get a large negative peak with presaturation, the pulse is probably too strong. Lower pl9 (or PLW9) in Watt or increase it in dB until you don't see a negative signal anymore. Question 3 answers Jan 23, 2019 I am looking to set up a Fragment based screening using STD NMR. Our NMR scientist is currently in the process of updating our topspin software to 3.6.1. Does anyone have and electronic version of the Topsin user manual for 3.6.1 so that I can educate myself on STD-NMR or alternatively a SOP. Relevant answer Peter J Cossar Jan 30, 2019 Answer Clemens Anklin, Thank you for these resources. The Bruker-fragment Based screening analysis is quite useful. Question 4 answers Dec 18, 2018 Hello all, The data shown here is a hypberbole to demonstrate a problem I've observed. Attached is an example of the phenomena I've observed. Not a problem, since all the peak labels are is a label right. Except that in cases where I adjust the PPRESOL to a higher integer. I was hoping to get rid of the shoulders of peaks. Instead, I'm observing an opposite effect where the shoulder is a lower intensity and is therefore picked first. Next, when I would expect the peak maximum to be picked, if it is within the 10 points that the PPRESOL defines, then the peak maximum is NOT picked at all. First, you set a relatively high MI and do the peak picking, then set it to a relatively low MI and execute it again. Perhaps it will then recognise that there is already a peak from the first stage, and not mark a peak in the second stage. This could easily be scripted as a macro, python, or au program. View 0 Recommendations How to convert multiple Topspin NMR files to a Matlab matrix. Question 2 answers Nov 7, 2018 Is there any matlab script I can use to convert (at once) multiple nmr files into a single matrix. Thanks! Relevant answer Teodoro S Kaufman Nov 11, 2018 Answer Dear Alexander, Thank you very much for your tip. It gave me a key clue and finally was able to make my own script based on one from the page you recommended. View 4 Recommendations How to interpret lineshape fitting data in TopSpin. Question 4 answers Nov 1, 2018 I am trying to analyse NMR peak width by fitting mixed Gaussian - Lorentzian shapes in TopSpin. In the results file the last column says Lor. chisq. This column usually displays two sets of numbers vertically stacked. One is always of the order 1exp(16) while the other is 100.00 I am unable to find out what these two numbers signify. Can anyone please elaborate what these denote. Kind regards Alfred View 0 Recommendations Bryn Monnery asked a question related to TopSpin Extracting y-axis from 2D plots in TopSpin Question 4 answers Sep 11, 2018 Dear all, I have a 2D NMR spectra and want to export the y-axis plot as a 1D spectra for further analysis. Is there an easy way of doing this. I currently have a ridiculous workaround that is very time consuming. Thanks. Relevant answer Wolfgang Baumann Sep 12, 2018 Answer Dear Bryn, I assume you want to process the projections separately. I was hoping to be able to convert between the two values, but there seems to be another factor in the relationship between the relative and absolute values, at least with respect to MI being a cutoff for peak picking. MI is a value relative and is related to plotting parameters. When pscal is set to global then CY will define the relative height of the largest peak. Clemens View 14 Recommendations How to script in blind regions for Topspin Auto-peak picking. I know it is possible in the GUI by defining the regions. Bonus question: Is it possible to retrieve the value of where your contour level currently is.gr-korea.com/upload/userfiles/2022/10/files/221019195859.pdf So that I can scroll to where I want to pick the peaks, and retrieve this intensity to set as the MI or MAXI value. I found some reference paper about 139La MAS, But some little bit confuse about pulse program. They use: t1-t- t3 spin-echo sequence with complex phase cycling. My question is that what is the pulse program name on the topspin software. There is pulse name like onepulse, or CP. However, in this case, there is no pulse name. Could you give me comment. Relevant answer Amrit Venkatesh Jul 12, 2018 Answer Hi Kyungduk. If you are interested in acquiring solid state NMR spectra of 139La, I would recommend using the QCPMG pulse sequence and acquiring static spectra. Once you have a static spectrum, it would be prudent to also record an MAS QCPMG spectrum to confirm the simulated quadrupole parameters. Alternatively, you can use the WURST-QCPMG technique to record static spectra at two fields. Can you share the reference for the pulse sequence you described. View 0 Recommendations How to set Topspin peak picking thresholds in serial processing. Question 6 answers Mar 20, 2018 I have designed a quick macro to go through and re-process a subset of my 2D data. Since I'm working with mixtures, the dynamic range of what I'm looking into can vary. Is there an automatic peak picking function compatible with topspin that would allow for better dynamic ranges of real peaks. Question 2 answers Mar 21, 2018 hi, all I am using topspin to do baseline correction of proton nmr spectrum.Is any one know what why this happens and how can I solve this problem. Thanks very much! Screen Shot 2018-03-21 at 17.26.28.png 1.10 MB Relevant answer A researcher Mar 22, 2018 Answer Yumeng, when you use this type of baseline correction you adjust the red line with the coefficients A - E until it matches the baseline of your spectrum. Then you click on the big triangle (DELTA) to see the spectrum with the correction applied. The you click on the save and return button. This should save the corrected spectrum. View 9 Recommendations How to apply deconvolution to more than one integral in TopSpin software. Question 3 answers Jan 17, 2018 I have a nmr spectrum with more than one compound and the peaks are overlapping, so I need to apply the deconvolution command to find out the shape and area of those peaks. But when I apply this command to an integral, I can not replicate to other integrals. Relevant answer A researcher Jan 22, 2018 Answer hello Monica, There are basically two ways to use deconvolution in Topspin. I can do it from the peak picking routine. First you peak pick your spectrum, then click on the big blue D. This will do the dewconvolution and you will see the list with all the peaks and integrals and finally the deconvolution result over the experimental spectrum. The other way is to do the integration first then over an itegral click the right mouse button and there you can also find deconvolution functions. View 4 Recommendations Can anyone help me for integral values of given H NMR spectrum.You can draw lines that approximately represent the area of the two small peaks as in the attached plot. The distance between the lines gives you the integral. Here the total is about 70 mm high on a plot on normal paper.If the paper thickness is uniform the weight of each peak represents the area. If the txt file you have is a JCAMP you can import it into Topsipn. View 5 Recommendations Srinivasa Rao Penumutchu asked a question related to TopSpin How to install user defined macro in TOPSPIN 3.5 ? Question 3 answers May 3, 2017 I have macro (abs.13c) from one of my friend that she got from bruker to correct the baseline after processing the 1d spectra. Clemens (author of the program) View 4 Recommendations Difference in Bruker proc and procs files. Is one created at the time of acquisition and another created and updated if I change these in topspin? 2. Where is the SR value stored. I have looked in Proc and Acqu files and have not found where this value changes when I change it in Topspin. Is this value calculated elsewhere. Relevant answer Maria Theresia Zich Oct 21, 2016 Answer Hi Joseph! 1.) To my knowledge, the s refers to status - the status files are written when you acquire or process. You acquire, TD 2048 is written to acqus. Within Topspin, you can see the Status parameters by clicking on the S in the ProcPars and AcquPars tab toolbar. 2.) Check for the SF value, it sets the spectrometer frequency and contains anything you add in SR. MT View 5 Recommendations Francois Bedard asked a question related to TopSpin Is it possible to do multiple solvent suppression for 2D NOESY with Bruker instrument. TFE-d2 is 99 and the peak is too high to acquire the 2Ds. We need 2D 1H TOCSY COSY NOESY. There is many experiments for the multiple peaks suppression as the double presaturation, excitation sculpting, WET, jump-return, etc. There is a preset for the parameters on Varian systems for the 2D 1H NOESY (with multiple solvents suppression) but I can only find TOCSY and COSY but not NOESY for Bruker. What is the most relevant procedure to make the suppression of H2O and TFE for a 2D 1H NOESY on a Bruker instrument please. Thanks Relevant answer Bhawna Chaubey May 24, 2016 Answer Yes, one can use biselective presaturation pulse for supression of these two solvents. View 7 Recommendations Temperature dependent NMR? Question 6 answers Mar 21, 2016 I want to do a temperature dependent NMR on my sample from 5C to 50C with an increment of 5C and time gap of 1hr 30min. Is there any method to automatise the NMR machine for the purpose. We have Topspin 3.x software. Relevant answer Steven Clemens Mar 24, 2016 Answer Rubin, thanks for asking this question. I too have been wondering if there is a way to do this, and I am intrigued by Bulat's answer (I was not aware of this program). I'm surprised that this is not included in the AU program by default. View 0 Recommendations After 1D NMR, how do I get list of metabolites after statistical analysis in metaboanalyst. Question 2 answers Oct 24, 2015 I did 1D NMR and I have analysed my results in topspin and statistical analysis in metaboanalyst 3.1. Zip folder result is attached. I want to know how I will get my list of metabolites from HMDB database. Thank u Downlo ad (1).zip 264.87 KB Relevant answer Bolaji F Oyeyemi Oct 30, 2015 Answer Thank you, it worked View 0 Recommendations Can anyone help with extraction J coupling from DQF COSY using TOPSPIN 3.0 Question 5 answers Oct 7, 2015 I cannot extract the 1D spectra from DQF COSY spectra of my sample to get the J coupling constant. Also iNMR is not working on my system. Can anyone suggest other ways to extract J coupling from DQF COSY. I would appreciate if anyone can give direction to do so using TOPSPIN. Thank you. Relevant answer A researcher Oct 13, 2015 Answer If you need to determine the coupling constants with high accuracy consider using a 1D selective COSY experiment with a large number of data points for the FID. View 5 Recommendations What is the purpose of file (or 'trigg' command) in Bruker NMR pulse program. Question 5 answers Sep 30, 2015 I am trying to use one pulse program in Topspin 2.3, but it's not working. The pulse program works in an earlier version of Topspin (probably version 1.1). But when I tried to use it in Topspin 2.3, it's showing compilation error. When I deactivated (by putting semicolon) these two lines, the program doesn't show any compilation error. Looks like it will work. Now I am concerned that, is it OK to use the pulse program without 'trigg' command or trigg include file. Is there any chance of damaging the probe. Thanks in advance! Relevant answer A researcher Oct 1, 2015 Answer the trigg command is only in there to provide a trigger for an oscilloscope. This was used to see the pulse sequence on a scope. It is perfectly safe to run it with the lines commented out. Clemens View 0 Recommendations Any advice on 2D-DOSY of small impurities in samples of oligosaccharides. In order to identify such impurities avoiding overlapping, I am trying to get 2D-DOSY with topspin. Unfortunately, such low intensity signals are not well-processed and they appear at the same row (diffusion coefficient) than the oligosaccharide. What parameters for acquiring and processing would be the best. Thank you Relevant answer A researcher Aug 4, 2015 Answer in order to separate the impurities with DOSY they need to have a different diffusion coefficient than the majore components in the mixture. If the impurities are also saccharides then there will be overlap of the signals. This requires a multicomponent fit in the DOSy calculation. You have to set the parameter Nexp (Number of components to fit) to 2 or three to allow for this. Even then you need a sizeable difference in diffusion coefficients to see the two. If the concentration of the impurity is too low not even this will help. If yo have aneough material and time then the DOSY-INEPT might be a solution. In this experiment you do the diffusion on Protons but then transfer the magnetization to Carbon. You most liekyl have a better dispersion of the signals in carbon. But here as well if the impurity is present in a very low concentration you might not see it. Question 3 answers Mar 23, 2015 I am trying to do a Sola Solid line shape analysis using Topspin NMR software in order to obtain some kinetic data from a VT-NMR experiment. However, I can not fit the curve. I keyed in Solaguide then the window appeared (attached file). Please advise. Thank you! Captur e.jpg 71.08 KB Relevant answer A researcher Apr 26, 2015 Answer Hi Mer, if you say kinetic data from a VT experiment do you mean exchange data. Is this from a liquids sample. In this case DNMR is better than sola. DNMR is described in the DNMR manual. For help on SOLA check chapter 6 of the structur analysis tools manual. Both manuals can be found under Help (?), Manuals, Analysis and Simulation. Clemens View 4 Recommendations How do you deconvolute an PGSE NMR diffusion spectra for diffusion analysis. Question 1 answer Jun 20, 2014 I am using Topspin 3.0 for analyzing the data of a PGSE NMR experiment. Two of the peaks are overlapped. Is there a way in topspin to deconvolute the individual spectra out of the 16 stacked spectra. I cannot integrate the overlapped peaks for diffusion analysis. I have tried the 'dcon' command after doing manual peak picking but its not very accurate. Can I extract these spectra as an CSV file such that I can use any other software programs for deconvolution. Relevant answer H. Douglas Morris Jun 24, 2014 Answer If dcon is not sufficient for your needs you can always export bruker data as ASCII using convbin2ascii. That will produce a file that you can chop up to fit in whatever program you wish. View 0 Recommendations Can anyone help with 1d NMR data processing in topspin. Question 5 answers May 2, 2014 I want to ask one question related to data processing in Topspin. I done 10 1-d diffusion experiments. Now I have to find the area under one peak(in all spectra) and then I have to plot it. After fitting in Stejesical Tanner equation I will find diffusion coefficient. I want to know that in Is there any internal program in topspin which can do it or I have to do it manually. Relevant answer H. Douglas Morris May 12, 2014 Answer Dear Satnam, If you have independently run a set of 1D experiments you may have to process the data outside of the Topspin environment for fitting your data. This is because the automation routines in Topspin need additional setup to do this automagically. Using Simplot to fit your peak area, then plot the peak area vs B-factor in your favorite spreadsheet, fit the S-T equation and you are set. Search for more research, methods, and experts in other areas on ResearchGate.