.
Category
- Spectroscopy and Spectrometry » NMR Spectroscopy
Booking Details
Facility Management Team and Location
Facility Features, Working Principle and Specifications
Facility Description
HF NMR 750 MHz available for both internal and external users from IIT Bombay and outsiders.
Features :
1)For solution-state NMR:5mm triple resonance H/C/N nuclei with 2H lock and 50G/cm gradient along Z axis.
2) For solid-state NMR:
3.2mm CP-MAS DVT triple resonance H/X/Y probe with max spinning speed of 24KHz
3.2mm CP-MAS triple resonance (H/C/N) E-free probe (Bio-solid) with max.spinning speed of 24KHz
1.9 mm H/C/N CP MAS triple resonance(H/C/N) probe with max. spinning speed of 42KHz
3)For wide-line static probes:
Low-temperature wide-line probe, solenoid coil
5mm and 7.5mm, can be tuned to various nuclei and can go upto 20K.
Working principle :
Nuclear Magnetic Resonance spectroscopy (NMR) is a one of the powerful and theoretically complex analytical technique. It is a spectroscopy where an ensemble of nuclei of atoms that possesses "magnetic moments" and "angular momentum" is subjected to an external magnetic field. As the nuclear angular momentum is quantized, these nuclei align either parallel or anti-parallel to the applied magnet field. Depending upon the nature of nuclei, one of these aligned states (in most cases, it is parallel) is more energetically favorable; that gives rise to net bulk magnetization. An external radiofrequency pulse is applied to the bulk magnetization to establish a resonance condition which in turn realigns bulk magnetization in the transverse plane of the external magnetic field. Ensemble of spins then precesses at a characteristic frequency and depending upon their chemical environment these precessional frequencies can be different for different chemical entity (Chmical shift). These ensemble of spin precessing in the magnetic field generates current which is a time decaying function as the spins restore their equilibrium states. Time domain signals are Fourier transformed to generate a frequency domain data which provide characteristic property of various chemical entities.
Bruker 750 WB MHz & its configuration :
Make and Model : Bruker Biospin Switzerland, Avance III 750 MHz
Magnetic Field : 17.61 Tesla, Wide bore (89 mm)
Host Computer : HP make Linux PC equipped with Intel Xenon Dual core W3505, 2, 53 GHz, 4 GB RAM, 500 GB Hard Disk, DVD-RW, 20inch TFT monitor
Software : Topspin 3.6.2 or higher for data processing and analysis
Instructions for Registration, Sample Preparation, User Instructions and Precautionary Measures
External Users can come in-person or send your samples along with a letter from the Head / Guide on your College/Institute /Industry Original Letter Head for registration stating that the analysis is for research purpose to qualify for academic concession. The letter should be addressed to The Convener, HFNMR central facility, IIT, Bombay.
The analytical data / spectra are provided only for research / development purposes. These cannot be used as certificates in legal disputes.
Samples, letter and payment should be sent in the same cover only. If Samples are received without covering letter/DD, the samples will be sent back to the user without any further intimation/notice.
These cost does not include analysis charges.
Please send the samples in quantity as mentioned. Samples are not recovered, unless a special request is made.
Radioactive materials will not be entertained.
Unstable and explosive compounds are not accepted.
The payment should be made in advance by only Demand Draft (DD) in favour of: " The Registrar, IIT Bombay."
The DD along with sample and covering letter should be sent to the Convener, HFNMR facility,Room No. 304, SAIF
Data transfer and data processing : Data will be stored on the server and can be transferred to any computer in the campus using FTP.
Topspin will be accessible from any computer in the IITB campus.
For any query, please contact HFNMR Lab, 304, SAIF, IIT Bombay or ashutoshk@iitb.ac.in
- For Liquid-state: Instrument can probe 1H, 13C and 15N only.
- Users are advised to bring 15-20 mg of sample depending upon its molecular weight for obtaining high resolution proton or carbon NMR spectra.
- The sample should be completely soluble in 600 µl of the given solvent.
- For water-soluble samples, 10% D_2O must be added.
- For Bio-molecular samples (Protein, peptide and nucleic acids): concentration should be >500 µM.
- For multi-nuclei bio-molecular experiments: Samples must be isotope labeled.
- For solid-state: For MAS-NMR experiments, sample should be in the form of very fine powder (20 microns) and at least 40-60 mg of powder is required.
- Bio-solid samples can be in jelly form.
- For multi-nuclei bio-molecular experiments: Samples must be isotope labeled.
Instructions for users :
First time users should contact the operator to understand the requirements.
Sample should be completely soluble in 600 μl of the given solvent.
For low molecular weight (MW < 250) compounds a minimum of 1-3 mg and for high molecular weight 2-5 mg of samples should be provided for proton spectra.
For protein samples, concentration should be minimum 500 ïM for 2D and 3D experiments.
For solid state NMR sample requirement is ~ 100 mgs.
For proton decoupled Carbon-13 spectra, 50-100 mg of sample will be required
Solvent Requirement :For ensuring magnetic field stability and adjusting field homogeneity, a deuterium lock channel is provided. Therefore, samples are to be dissolved in a deuterated solvent. Deuterated solvents like D2O, CDCl3, are provided by the Facility free of cost. However Users have to pay for expensive solvents such as CD3COCD3, DMSOd6, C6D6, etc.. The User should check the solubility of the sample in any of these solvents (of course, in undeuterated solvent) and suggest best solvent.
Charges for Analytical Services in Different Categories
Applications
Experiments can be performed with wide temperature range.
A series on nD experiments can be performed in the liquid phase.
Suitable for multi-nuclei, multi-dimensional MAS experiments.
Static solids can be investigated at various temperature (up to 20K).
Sample Details
Non Toxic, Non flammable and Non magnetic
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SOP, Lab Policies and Other Details
Publications
2022-23
Dey A, Mitra D, Rachineni K, Paithankar H, Khatri LR, Vajpai N, Kumar A*. Mapping of methyl epitopes of a peptide-drug with its receptor by 2D STDD-Methyl TROSY NMR. Chembiochem. 2022 Oct 13. doi: 10.1002/cbic.202200489. Epub ahead of print. PMID: 36227643.
2. Shukla, Shivangi, and Ashutosh Kumar. Centromere Chromatin Dynamics at a Glance. Epigenomes 6, no. 4 (2022): 39.doi:10.3390/epigenomes6040039.
3. Shukla S, Agarwal P, Kumar A. Disordered regions tune order in chromatin organization and function. Biophys Chem. 2022 Feb;281:106716. doi: 10.1016/j.bpc.2021.106716. Epub 2021 Nov 17. PMID: 34844028.
4. Singh JS, Sajeev T K, Panigrahi R, Cherry P, Panchakshari NA, Shukla VK, Kumar A*, Mishra RK. Implications of critical node-dependent unidirectional cross-talk of Plasmodium SUMO pathway proteins. Biophys J. 2022 Apr 19;121(8):1367-1380. doi: 10.1016/j.bpj.2022.03.022. Epub 2022 Mar 21. PMID: 35331687; PMCID: PMC9072691.
5. Agadi N, Maity A, Jha AK, Chakrabarti R, Kumar A. Distinct mode of membrane interaction and disintegration by diverse class of antimicrobial peptides. Biochim Biophys Acta Biomembr 2022 Dec 1;1864(12):184047. doi: 10.1016/j.bbamem.2022.184047. Epub 2022 Sep 12. PMID: 36100074.
6. Bhattacharya A, Shukla VK, Kachariya N, Preeti, Sehrawat P, Kumar A. Disorder in the Human Skp1 Structure is the Key to its Adaptability to Bind Many Different Proteins in the SCF Complex Assembly. J Mol Biol. 2022 Sep 15;434(21):167830. doi: 10.1016/j.jmb.2022.167830. Epub ahead of print. PMID: 36116539.
7. Soumya Ranjan Pujahari, Pramod S. Mali, Rudra N. Purusottam, Ashutosh Kumar Combined liquid-state and solid-state NMR at natural abundance for comparative HOS assessment in the formulated-state of biphasic Biopharmaceutics. https://doi.org/10.1021/acs.analchem.2c05485
8. Sreya Das, Navin Khaneja, ``Composite pulse combinations for chirp excitation'' Journal of Magnetic Resonance , 347, 107359, (2022).
9. Sreya Das, Justin Jacob, Navin Khaneja, ``Mechanism of chirp excitation'' Journal of Magnetic Resonance Open , Volumes 10-11, 100026, (2022).
10. Manoj Gautam, Govind Kumar Mishra,Aakash Ahuja,Supriya Sau,Mohammad Furquan,Sagar Mitra‘Direct-Contact Prelithiation of Si–C Anode Study as a Function of Time, Pressure, Temperature, and the Cell Ideal Time”
11. S Yadav, AK Sam, C Venkataraman, A Kumar, HC Phuleria, “1H NMR structural signatures of source and atmospheric organic aerosols in India” Chemosphere 301, 134681
12. A Anand, S Yadav, HC Phuleria, “Chemical characteristics and oxidative potential of indoor and outdoor PM2. 5 in densely populated urban slums” Environmental Research 212, 113562
2021-22
1. Joshi S, Khatri L K, Kumar A*, Rathore S A. Monitoring size and oligomeric-state distribution of therapeutic mAbs by NMR and DLS: Trastuzumab as a case study J Pharm Biomed Anal 2021, 195, 113841. doi: 10.1016/j.jpba.2020.113841
2. Joshi S, Khatri L K, Kumar A*, Rathore S A. NMR based quality evaluation of mAb therapeutics: A proof of concept higher order structure biosimilarity assessment of trastuzumab biosimilars J Pharm Biomed Anal 2022, 214, 114710 doi:/10.1016/J.JPBA.2022.114710
3. Khosravi F, Upadhyay M, Kumar A, Shahsavani MB, Akbarian M, Najafi H, Tamaddon AM, Yousefi R. A novel method for the chaperone aided and efficient production of human proinsulin in the prokaryotic system J Biotechnol. 2022 Feb 20;346:35-46. doi:10.1016/j.jbiotec.2022.01.002. Epub 2022 Jan 21.PMID: 35066065
4. Sarkar S, Purusottom N R, Kumar A, Khaneja N. Chirp pulse sequences for broadband π rotation J Magn Reson. 2021, 38, 107002. doi: 10.1016/j.jmr.2021.107002
5. Pravin N, Kumar R, Tripathi S, Kumar P, Mohite GM, Navalkar A, Panigrahi R, Singh N, Gadhe LG, Manchanda S, Shimozawa M, Nilsson P, Johansson J, Kumar A, Maji SK, Shanmugam M. Benzimidazole‐based Fluorophores for the Detection ofAmyloid Fibrils with Higher Sensitivity than Thioflavin‐T J. Neurochem. 2021, 156(6), 1003-1019. doi: 10.1111/jnc.15138
6. Marathe S, Dhamija B, Kumar S, Jain N, Ghosh S, Dharikar JP, Srinivasan S, Das S, Sawant A, Desai S, Khan F, Syiemlieh A, Munde M, Nayak C, Gandhi M, Kumar A, Srivastava S, Venkatesh KV, Barthel SR, Purwar R. (2021) Multiomics Analysis and Systems Biology Integration Identifies the Roles of IL-9 in Keratinocyte Metabolic Reprogramming. J Invest Dermatol. doi: 10.1016/j.jid.2021.02.013.
7. AS Sawner, S Ray, P Yadav, S Mukherjee, R Panigrahi, M Poudyal, K Patel, D Ghosh, E Kummerant, A Kumar, R Riek and SK Maji (2021), Modulating α-Synuclein Liquid–Liquid Phase Separation. Biochemistry, 60(48): 3676-3696
8. Singh JS, Sajeev TK, Panigrahi R, Shukla VK, Kumar A*, Mishra RK Implications of critical nodes-dependent unidirectional cross-talk between Plasmodium and Human SUMO pathway proteins in Plasmodium infection Biophy. J.(2022) https://doi.org/10.1016/j.bpj.2022.03.022
2017-18
1. Dubey R, Minj P, Malik N, Sardesai DM, Kulkarni SH, Acharya JD, Bhavesh NS, Sharma S, Kumar A (2017) Recombinant human islet amyloid polypeptide forms shorter fibrils and mediates β-cell apoptosis via generation of oxidative stress. Biochem J. 16:3915-3934
2. Jha NN, Kumar R, Panigrahi R, Navalkar A, Ghosh D, Sahay S, Mondal M, Kumar A Maji SK (2017) Comparison of α-Synuclein Fibril Inhibition by Four Different Amyloid Inhibitors. ACS Chem Neurosci DOI:10.1021/acschemneuro.7b00261
3. Ranjan P, Kumar A (2017) Perturbation in long-range contacts modulates kinetics of amyloid formation in α-Synuclein familial mutants. ACS Chem. Neurosci. 18: 2235-2246
4. Khaneja N, Kumar A (2017) Two pulse recoupling. J Magn Res 281: 162-171.
5. Khaneja N, Kumar A (2017) Broadband excitation by method of double sweep. Applied MagnRes 281: 162-171
6. Shukla VK, Singh JS, Vispute N, Ahmad B, Kumar A, Hosur RV (2017) A functionally relevantintermediate in the unfolding pathway of Cyclophilin. Biophysical J 112: 605-619
7. Ranjan P, Ghosh D, Yarramala DS, Maji SK, Kumar A (2017) Differential copper binding to alphasynucleinand its disease-associated mutants affect the aggregation and amyloid formation. Biochim Biophys Acta 1861: 365-374
8. N. Khaneja, Chirp excitation Journal of Magnetic Resonance 282, 32-36 (2017).
9. N. Khaneja, Electron dynamics in solid state via time varying wavevectors Physica B 539, 29-34 (2018).
10. N. Khaneja, Chirp Mixing Chemical Physics Letters 704, 62-67 (2018) 11. N. Khaneja, Conservation of Energy, Density of States and Spin Lattice relaxation Concepts in Magnetic Resonance: Part A (2018) https://doi.org/10.1002/cmr.a.21457
2016-17
1.Khaneja N and Kumar A, "Two Pulse Recoupling" Journal of Magnetic Resonance 281, 162-171 (2017).
2. Khaneja N and Kumar A, "Broadband excitation by method of double sweep", Applied Magnetic Resonance 48(8), 771-782 (2017).
3. Khaneja N "Rf-inhomogeneity compensation using method of Fourier synthesis" Journal of Magnetic Resonance, 277, 113-116 (2017).
4. Ranjan P, Ghosh D, Yarramala DS, Maji SK, Kumar A (2017) Differential copper binding to alpha-synuclein and its disease-associated mutants affect the aggregation and amyloid formation Biochim Biophys Acta 1861: 365-374
5. Khaneja N, Kumar A (2016) Four pulse recoupling. J Magn Res 272: 158-165.
6. Singh JS, Shukla VK, Gujrati M, Mishra RK, Kumar A (2016) Backbone and side chain resonance assignments of Plasmodium falciparum SUMO. Biomol NMR Assign 11(1):17-20. doi: 10.1007/s12104-016-9712-9.
7. Sagar N, Singh AK, Temgire MK, Vijayalaxmi S, Dhawan A, Kumar A, Chattopadhyay N, Bellare JR (2016) 3D scaffold induces efficient bone repair: in vivo studies of ultra-structural architecture at the interface. RSC Advance
8. Jacob RS, Das S, Ghosh S, Anoop A, Jha NN, Khan T, Singru P, Kumar A, Maji SK (2016) Amyloid formation of growth hormone in presence of zinc: Relevance to its storage in secretory granules. Sci Rep 23; 6:23370
9. Khaneja N, Kumar A (2016) Recoupling Pulse Sequences with Constant Phase Increments. J Magn Res 271:75-82
10. Malik N, Kumar A (2016) Resonance assignment of disordered protein with repetitive and overlapping sequence using combinatorial approach reveals initial structural propensities and local restrictions in the denatured state. J Biomol NMR 66:21-35
11. Kachariya NN, Dantu SC, Kumar A (2016). Backbone and side-chain assignments of human cell-cycle regulatory protein Skp1. Biomol NMR Assignment
12. Ranjan P, Kumar A (2016). The Involvement of His50 during Protein Disulfide Isomerase binding is essential for inhibiting α-Syn fibril formation. Biochemistry 55(19): 2677-80.
13. Shukla VK, Singh JS, Trivedi D, Hosur RV, Kumar A (2016). NMR assignments of mitochondrial cyclophilin Cpr3 from Saccharomyces cerevisiae. Biomol NMR Assign 10(1): 203-6.
14. Singh AK, Gajiwala AL, Rai RK, Khan P, Singh C, Barbhuyan T, Vijayalakshmi S, Chattopadhyay N, Sinha N, Kumar A, Bellare JB (2016). Cross-correlative 3D micro-structural investigation of human bone processed into bone allografts. Mater Sci Eng C Mater Biol Appl 62: 574-84.