Prof. Wolfgang Voelter Laboratories Complex (NRL)
A research wing of the H.E.J. Research Institute of Chemistry is focusing on applied chemical science, textile chemistry, nanochemistry and other disciplines of national need. The Executive Board of ICCBS approved that the New Research Laboratory (NRL) of the ICCBS will be named as the Prof. Wolfgang Voelter Laboratories Complex, in recognition of his outstanding services to the ICCBS and Pakistan, spread over 5 decades.
Prof. Wolfgang Voelter is among those individuals who have left an indelible mark on science in Pakistan and in many other developing countries. He was born in October 20, 1936 in Ludwigsburg, Germany, and completed Diploma in Chemistry in 1956 from Tübingen University. He also got degree in Vorphysikum in Medicine (1964) and Dr. rer. nat. (1966) from Tübingen University (Prof. Ernst Bayer). In parallel, he finished Physikum in Medicine at the Erlangen University. He has worked as a Research Fellow at Stanford University (Prof. Carl Djerassi) and Kaiser Foundation Research Institute, California, USA, from 1966-1970. Since 1970 he is associated with Tübingen University as a Professor.
He first visited Pakistan in September 1974, and met Professors Salimuzaman Siddiqui FRS and Atta-ur-Rahman FRS at the Department of Chemistry, University of Karachi. He convinced German Government and GTZ to approve an initial allocation of 2.3 million DM, followed by another allocation of 3.5 million DM. This allowed H. E.J. Research Institute of Chemistry, to acquire sophisticated equipment, such as mass (MS), nuclear magnetic resonance (NMR), circular dichorism (CD) instruments, and further laboratory equipment, chemicals, and text books.
Prof. Voelter has trained and supported a large number of young Pakistanis in their careers as a true mentor. Approximately 40 Pakistani scientists, students, and technicians have got advance research training in the esteemed laboratory of Prof. Wolfgang Voelter, including 20 full Ph.Ds. Over 90 German students from his laboratory have also visited the HEJRIC to carry out part of their Diploma work. Over 150 research publications in best peer reviewed journals have been published in collaboration with the laboratory of Prof. Wolfgang Voelter.
The Nuclear Magnetic Resonance (NMR) Facility at the ICCBS is a Core Science Facility established in 1982. It provides access to qualified researchers in the physical, biological, and industrial sciences to state-of-the-art NMR instrumentation for spectroscopy. The Facility serves mostly undergraduate, graduate and post-doctoral researchers in the Chemistry and Chemical and Biomolecular Engineering Departments all over the country.
The Facility presently operates thirteen superconducting NMR spectrometers (Bruker) of varying purposes and capabilities, including four instruments (one 800 MHz two 600 MHz and one 500 MHz) are equipped with cryogenically cooled probes, and one multinuclear probe to detect all type of elements. The new 800 MHz NMR instrument has recently been installed. The NMR instruments are accessible to trained users 24 hours per day, year-round.
The Facility also serve corporate and industrial clients, we offer a full range of NMR spectroscopy service options from routine 1D proton spectra acquisition and interpretation to complex 2D NMR analysis for the verification of their products as well as contaminants.
Welcome to the website for the mass spectrometry center at the HEJ Research Institute of Chemistry at the University of Karachi. This laboratory has instrumentation and expertise for performing a wide range of mass spectrometry measurements. This web site provides basic information required for submitting samples for analysis, as well as a tutorial on available ionization methods and interpretation of results.
The information provided here is directed to the analyses of compounds with molecular weights less than approximately 1000 a.m.u.. Synthetic materials and natural products will generally be in this category. Mass spec analyses of higher molecular weight materials, such as proteins, their digests, oligosaccharides and oligonucleotides are also possible, but may require special consideration. More detailed information on mass spec. analyses of both low-and high-molecular weight materials may be obtained directly from the MS lab staff at firstname.lastname@example.org
ONE JEOL JMS HX-110 with GC.
TWO JEOL JMS -600H with GC.
ONE VARIAN MAT 312.
1. Electronic Impact (EI)
2. Chemical Ionization (CI)
3. Fast Atom Bombardment (FAB)
4. Gas Chromatograpy Mass Spec (GC-MS)
5. Atmospheric Pressure Chemical Ionization (APCI)
6. Electro Spray Ionization (ESI)
7. Ion Spray
8. Nano Spray
9. Matrix Assisted laser Desorption Ionization (MALDI)
10.Liquid Chromatography - Mass Spectroscopy (LC-MS) with E.S.I.
Unless samples are introduced into the mass spectrometer by either gas or liquid chromatography, samples with multiple components generally give complicated mass spectra that are difficult to interpret reliably. The purity of all samples should be assessed by NMR and/or chromatography prior to submission for mass spec analysis. Impurities are especially important for ESI and FAB analyses because one component can suppress the signal for another component. Signal suppression may vary with the amount of sample used for analysis, with less sample often leading to less suppression. Finding different peaks in a spectrum when the same sample is analyzed multiple times may indicate that the sample contains multiple components.
Good sample preparation procedures are essential for good mass spec analyses. Common sources of problems include contamination by materials extracted from containers, vials, tubing etc. used to prepare or store the sample. Organic solvents can extract plasticizer from many plastic containers.
EI mass spectra of common phthalate plasticizers have peaks at (ask Yaqub John for masses). Acidic solutions can extract large quantities of Na+, K+, etc. from soft glass containers. These salts can be highly detrimental for ESI and FAB analyses. Concentration of large volumes of solvent makes this problem much worse. High concentrations of salt can often be detected by a high abundance of sodium or potassium adducts in ESI and FAB spectra.
In the case of FAB, these cations can replace the proton in matrix cluster ions. For example, the sodium adduct of the glycerol matrix peak at m/z 185 has an m/z of 207. In general, peaks differing in mass by 22 or 38 mu usually indicate sodium or potassium adducts, respectively. High concentrations of salt can be removed by reversed phase HPLC, or by similar solid phase extraction procedures using Sep-Paks or Zip-Tips.
Although picogram quantities of many compounds can be detected by mass spectrometry, it is useful to have at least 0.1 mg of material submitted. The quality of ESI and FAB spectra depends very much on the amount of sample introduced into the mass spectrometer. Too much or too little sample may lead to unsuccessful analyses. In the case of ESI, we request that you submit exactly 0.1 mg of material. Since sample introduction into the mass spectrometer usually requires dissolving the sample in a suitable solvent, it is essential that you indicate which common solvents will dissolve your sample.
|MASS SPECTROMETRY SAMPLE SUBMISSION FORMS:|
External Sample Submission Form H.E.C / Private Analysis
Internal FORM HEJ MASS LAB
Internal FORM-ESI-TWC MASS LAB
Internal FORM-MALDI-TWC MASS LAB
Note: Handling charges will have to be 15% beside the above rates
Mr. Yaqub John
Incharge Mass Spectroscopic Facility
UAN: 111-222-292, Ph: (+92-21) 4824925, 4824924, 4819010,
4824934,4824901,4824930 Ext: 103
Mr. Danish Idris
UAN: 111-222-292, Cell: 0092-321-2067822 Ph: (+92-21) 4824925, 4824924,
4819010, 4824934,4824901,4824930 Ext: 203
Single-Crystal X-Ray Diffraction Facility
Our X-ray laboratories located at the H. E. J. Research Institute of Chemistry and Prof. Dr. Atta-ur-Rahman Laboratories, have Bruker SMART APEX II Diffractometer and Bruker D8 VENTURE, respectively. The Bruker SMART APEX II is equipped with CCD detector and Mo X-ray source. Whereas, D8 VENTURE is equipped with new PHOTON-100 CMOS detector, high brilliance Cu microfocus X-ray sources, Oxford cryosystem low temperature device, and PROTEUM3, software for structure elucidation of biomolecules.
Both laboratories are facilitating the collaborators both national and international levels in crystal structure determinations of small organic, inorganic molecules including absolute structure determination of small biologically active compounds and macromolecules, including protein-ligand complexes.