Gareth A. Morris

Last updated

Gareth Morris

FRS
Professor Gareth Morris FRS.jpg
Gareth Morris at the Royal Society admissions day in 2014
Born
Gareth Alun Morris

(1954-07-06) 6 July 1954 (age 69) [1]
Education Royal Grammar School, Newcastle upon Tyne
Alma mater University of Oxford (MA, DPhil)
Known for
Awards
Scientific career
Fields NMR spectroscopy [4]
Institutions University of Manchester
Thesis New techniques in fourier transform nuclear magnetic resonance  (1978)
Doctoral advisor Ray Freeman [5]
Website manchester.ac.uk/research/gareth.morris

Gareth Alun Morris FRS [6] (born 6 July 1954) is a Professor of Physical Chemistry, in the School of Chemistry at the University of Manchester. [4] [7] [8] [9] [10] [11] [12]

Contents

Education

Morris was educated at the Royal Grammar School, Newcastle and the University of Oxford where he was a student of Magdalen College, Oxford. [1] He was awarded a Master of Arts degree followed by a Doctor of Philosophy degree in 1978. [5]

Research

Research in the NMR lab along with Mathias Nilsson, Jordi Burés and Ralph Adams involves the development of novel nuclear magnetic resonance spectroscopy techniques, and their application to problems in chemistry, biochemistry, and medicine.

Awards and honours

Morris was elected a Fellow of the Royal Society (FRS) in 2014. His nomination reads:

Gareth Morris is one of the world's foremost innovators in high resolution nuclear magnetic resonance spectroscopy, and has had a major influence on the determination of chemical structure by NMR. Almost all commercial NMR spectrometers contain hardware and software that he originated, including deuterium gradient shimming (now standard on commercial spectrometers) and ingenious pulse sequences such as DANTE (the prototypical selective excitation sequence) and INEPT (now a key component of multidimensional NMR techniques, including many of those used for protein 3D structure determination). The impact and wide applicability of Morris's contributions have made them indispensable components of the state-of-the-art NMR toolkit. [6]

Morris received the James Shoolery Award 2015 awarded by SMASH (Small molecule NMR conference):

It is hard to imagine an NMR laboratory in the world which is not influenced daily by his developments from the foundations of INEPT and DANTE, through to modern gradient shimming, DOSY and pure shift methods. [13]

Related Research Articles

In nuclear magnetic resonance (NMR) spectroscopy, the chemical shift is the resonant frequency of an atomic nucleus relative to a standard in a magnetic field. Often the position and number of chemical shifts are diagnostic of the structure of a molecule. Chemical shifts are also used to describe signals in other forms of spectroscopy such as photoemission spectroscopy.

<span class="mw-page-title-main">Nuclear magnetic resonance spectroscopy</span> Laboratory technique

Nuclear magnetic resonance spectroscopy, most commonly known as NMR spectroscopy or magnetic resonance spectroscopy (MRS), is a spectroscopic technique to observe local magnetic fields around atomic nuclei. This spectroscopy is based on the measurement of absorption of electromagnetic radiations in the radio frequency region from roughly 4 to 900 MHz. Absorption of radio waves in the presence of magnetic field is accompanied by a special type of nuclear transition, and for this reason, such type of spectroscopy is known as Nuclear Magnetic Resonance Spectroscopy. The sample is placed in a magnetic field and the NMR signal is produced by excitation of the nuclei sample with radio waves into nuclear magnetic resonance, which is detected with sensitive radio receivers. The intramolecular magnetic field around an atom in a molecule changes the resonance frequency, thus giving access to details of the electronic structure of a molecule and its individual functional groups. As the fields are unique or highly characteristic to individual compounds, in modern organic chemistry practice, NMR spectroscopy is the definitive method to identify monomolecular organic compounds.

<span class="mw-page-title-main">Solid-state nuclear magnetic resonance</span>

Solid-state NMR (ssNMR) spectroscopy is a technique for characterizing atomic level structure in solid materials e.g. powders, single crystals and amorphous samples and tissues using nuclear magnetic resonance (NMR) spectroscopy. The anisotropic part of many spin interactions are present in solid-state NMR, unlike in solution-state NMR where rapid tumbling motion averages out many of the spin interactions. As a result, solid-state NMR spectra are characterised by larger linewidths than in solution state NMR, which can be utilized to give quantitative information on the molecular structure, conformation and dynamics of the material. Solid-state NMR is often combined with magic angle spinning to remove anisotropic interactions and improve the resolution as well as the sensitivity of the technique.

Carbon-13 (C13) nuclear magnetic resonance is the application of nuclear magnetic resonance (NMR) spectroscopy to carbon. It is analogous to proton NMR and allows the identification of carbon atoms in an organic molecule just as proton NMR identifies hydrogen atoms. 13C NMR detects only the 13
C
isotope. The main carbon isotope, 12
C
is not detected. Although much less sensitive than 1H NMR spectroscopy, 13C NMR spectroscopy is widely used for characterizing organic and organometallic compounds.

The heteronuclear single quantum coherence or heteronuclear single quantum correlation experiment, normally abbreviated as HSQC, is used frequently in NMR spectroscopy of organic molecules and is of particular significance in the field of protein NMR. The experiment was first described by Geoffrey Bodenhausen and D. J. Ruben in 1980. The resulting spectrum is two-dimensional (2D) with one axis for proton (1H) and the other for a heteronucleus, which is usually 13C or 15N. The spectrum contains a peak for each unique proton attached to the heteronucleus being considered. The 2D HSQC can also be combined with other experiments in higher-dimensional NMR experiments, such as NOESY-HSQC or TOCSY-HSQC.

Two-dimensional nuclear magnetic resonance spectroscopy is a set of nuclear magnetic resonance spectroscopy (NMR) methods which give data plotted in a space defined by two frequency axes rather than one. Types of 2D NMR include correlation spectroscopy (COSY), J-spectroscopy, exchange spectroscopy (EXSY), and nuclear Overhauser effect spectroscopy (NOESY). Two-dimensional NMR spectra provide more information about a molecule than one-dimensional NMR spectra and are especially useful in determining the structure of a molecule, particularly for molecules that are too complicated to work with using one-dimensional NMR.

Insensitive nuclei enhancement by polarization transfer (INEPT) is a signal enhancement method used in NMR spectroscopy. It involves the transfer of nuclear spin polarization from spins with large Boltzmann population differences to nuclear spins of interest with lower Boltzmann population differences. INEPT uses J-coupling for the polarization transfer in contrast to Nuclear Overhauser effect (NOE), which arises from dipolar cross-relaxation. This method of signal enhancement was introduced by Ray Freeman in 1979. Due to its usefulness in signal enhancement, pulse sequences used in heteronuclear NMR experiments often contain blocks of INEPT or INEPT-like sequences.

<span class="mw-page-title-main">Spin echo</span> Response of spin to electromagnetic radiation

In magnetic resonance, a spin echo or Hahn echo is the refocusing of spin magnetisation by a pulse of resonant electromagnetic radiation. Modern nuclear magnetic resonance (NMR) and magnetic resonance imaging (MRI) make use of this effect.

Fast low angle shot magnetic resonance imaging is a particular sequence of magnetic resonance imaging. It is a gradient echo sequence which combines a low-flip angle radio-frequency excitation of the nuclear magnetic resonance signal with a short repetition time. It is the generic form of steady-state free precession imaging.

Herbert Sander Gutowsky was an American chemist who was a professor of chemistry at the University of Illinois Urbana-Champaign. Gutowsky was the first to apply nuclear magnetic resonance (NMR) methods to the field of chemistry. He used nuclear magnetic resonance spectroscopy to determine the structure of molecules. His pioneering work developed experimental control of NMR as a scientific instrument, connected experimental observations with theoretical models, and made NMR one of the most effective analytical tools for analysis of molecular structure and dynamics in liquids, solids, and gases, used in chemical and medical research, His work was relevant to the solving of problems in chemistry, biochemistry, and materials science, and has influenced many of the subfields of more recent NMR spectroscopy.

In vivo magnetic resonance spectroscopy (MRS) is a specialized technique associated with magnetic resonance imaging (MRI).

Raymond Freeman FRS was a British chemist and professor at Jesus College, Cambridge who made important contributions to NMR spectroscopy.

<span class="mw-page-title-main">Nuclear magnetic resonance</span> Spectroscopic technique based on change of nuclear spin state

Nuclear magnetic resonance (NMR) is a physical phenomenon in which nuclei in a strong constant magnetic field are perturbed by a weak oscillating magnetic field and respond by producing an electromagnetic signal with a frequency characteristic of the magnetic field at the nucleus. This process occurs near resonance, when the oscillation frequency matches the intrinsic frequency of the nuclei, which depends on the strength of the static magnetic field, the chemical environment, and the magnetic properties of the isotope involved; in practical applications with static magnetic fields up to ca. 20 tesla, the frequency is similar to VHF and UHF television broadcasts (60–1000 MHz). NMR results from specific magnetic properties of certain atomic nuclei. Nuclear magnetic resonance spectroscopy is widely used to determine the structure of organic molecules in solution and study molecular physics and crystals as well as non-crystalline materials. NMR is also routinely used in advanced medical imaging techniques, such as in magnetic resonance imaging (MRI).

<span class="mw-page-title-main">Physics of magnetic resonance imaging</span> Overview article

The physics of magnetic resonance imaging (MRI) concerns fundamental physical considerations of MRI techniques and technological aspects of MRI devices. MRI is a medical imaging technique mostly used in radiology and nuclear medicine in order to investigate the anatomy and physiology of the body, and to detect pathologies including tumors, inflammation, neurological conditions such as stroke, disorders of muscles and joints, and abnormalities in the heart and blood vessels among others. Contrast agents may be injected intravenously or into a joint to enhance the image and facilitate diagnosis. Unlike CT and X-ray, MRI uses no ionizing radiation and is, therefore, a safe procedure suitable for diagnosis in children and repeated runs. Patients with specific non-ferromagnetic metal implants, cochlear implants, and cardiac pacemakers nowadays may also have an MRI in spite of effects of the strong magnetic fields. This does not apply on older devices, and details for medical professionals are provided by the device's manufacturer.

Triple resonance experiments are a set of multi-dimensional nuclear magnetic resonance spectroscopy (NMR) experiments that link three types of atomic nuclei, most typically consisting of 1H, 15N and 13C. These experiments are often used to assign specific resonance signals to specific atoms in an isotopically-enriched protein. The technique was first described in papers by Ad Bax, Mitsuhiko Ikura and Lewis Kay in 1990, and further experiments were then added to the suite of experiments. Many of these experiments have since become the standard set of experiments used for sequential assignment of NMR resonances in the determination of protein structure by NMR. They are now an integral part of solution NMR study of proteins, and they may also be used in solid-state NMR.

Nitrogen-15 nuclear magnetic resonance spectroscopy is a version of nuclear magnetic resonance spectroscopy that examines samples containing the 15N nucleus. 15N NMR differs in several ways from the more common 13C and 1H NMR. To circumvent the difficulties associated with measurement of the quadrupolar, spin-1 14N nuclide, 15N NMR is employed in samples for detection since it has a ground-state spin of ½. Since14N is 99.64% abundant, incorporation of 15N into samples often requires novel synthetic techniques.

<span class="mw-page-title-main">Geoffrey Bodenhausen</span> French chemist

Geoffrey Bodenhausen is a French chemist specializing in nuclear magnetic resonance, being highly cited in his field. He is a Corresponding member of the Royal Netherlands Academy of Arts and Sciences and a Fellow of the American Physical Society. He is professeur émérite at the Department of Chemistry at the École Normale Supérieure (ENS) in Paris and professeur honoraire at the Laboratory of Biomolecular Magnetic Resonance of the École Polytechnique Fédérale de Lausanne (EPFL). He is a member of the editorial board of the journal Progress in Nuclear Magnetic Resonance Spectroscopy. He is the chair of the editorial board of the journal Magnetic Resonance.

The Russell Varian Prize was an international scientific prize awarded for a single, high-impact and innovative contribution in the field of nuclear magnetic resonance (NMR), that laid the foundation for the development of new technologies in the field. It honored the memory of Russell Varian, the pioneer behind the creation of the first commercial NMR spectrometer and the co-founder, in 1948, of Varian Associates, one of the first high-tech companies in Silicon Valley. The prize carried a monetary award of €15,000 and it was awarded annually between the years 2002 and 2015 by a committee of experts in the field. The award ceremony alternated between the European Magnetic Resonance (EUROMAR) Conference and the International Council on Magnetic Resonance in Biological Systems (ICMRBS) Conference. Originally, the prize was sponsored by Varian, Inc. and later by Agilent Technologies, after the latter acquired Varian, Inc. in 2010. The prize was discontinued in 2016 after Agilent Technologies closed its NMR division.

Malcolm Harris Levitt is a British physical chemist and nuclear magnetic resonance (NMR) spectroscopist. He is Professor in Physical Chemistry at the University of Southampton and was elected a Fellow of the Royal Society in 2007.

Mathias Nilsson is a Swedish chemist and a Professor in the Department of Chemistry at The University of Manchester. His research in general is based on physical chemistry and analytical chemistry, specifically on development and application of novel methods in Liquids NMR Spectroscopy

References

  1. 1 2 Anon (2015). "Morris, Prof. Gareth Alun" . Who's Who (online Oxford University Press  ed.). A & C Black. doi:10.1093/ww/9780199540884.013.U281964.(Subscription or UK public library membership required.)
  2. Brown, J. M.; Chaloner, P. A.; Morris, G. A. (1987). "The catalytic resting state of asymmetric homogeneous hydrogenation. Exchange processes delineated by nuclear magnetic resonance saturation-transfer (DANTE) techniques". Journal of the Chemical Society, Perkin Transactions 2 (11): 1583. doi:10.1039/P29870001583.
  3. Morris, G. A. (1980). "Sensitivity enhancement in nitrogen-15 NMR: Polarization transfer using the INEPT pulse sequence". Journal of the American Chemical Society. 102: 428–429. doi:10.1021/ja00521a097.
  4. 1 2 Gareth A. Morris publications indexed by Google Scholar OOjs UI icon edit-ltr-progressive.svg
  5. 1 2 Morris, Gareth Alun (1978). New techniques in fourier transform nuclear magnetic resonance (DPhil thesis). University of Oxford.
  6. 1 2 "Professor Gareth Morris FRS". London: The Royal Society. Archived from the original on 2 May 2014.
  7. Morris, G. A.; Freeman, R (2011). "Selective excitation in Fourier transform nuclear magnetic resonance. 1978". Journal of Magnetic Resonance. 213 (2): 214–43. doi:10.1016/j.jmr.2011.08.031. PMID   22152346.
  8. Gareth A. Morris publications indexed by the Scopus bibliographic database. (subscription required)
  9. Morris, G. A.; Freeman, R. (1979). "Enhancement of nuclear magnetic resonance signals by polarization transfer". Journal of the American Chemical Society. 101 (3): 760–762. doi:10.1021/ja00497a058.
  10. Bodenhausen, G.; Freeman, R.; Morris, G. A. (1976). "A simple pulse sequence for selective excitation in Fourier transform NMR". Journal of Magnetic Resonance. 23 (1): 171–175. Bibcode:1976JMagR..23..171B. doi:10.1016/0022-2364(76)90150-5.
  11. Bax, A.; Morris, G. A. (1981). "An improved method for heteronuclear chemical shift correlation by two-dimensional NMR" (PDF). Journal of Magnetic Resonance. 42 (3): 501–505. Bibcode:1981JMagR..42..501B. doi:10.1016/0022-2364(81)90272-9.
  12. Pelta, M. D.; Barjat, H.; Morris, G. A.; Davis, A. L.; Hammond, S. J. (1998). "Pulse sequences for high-resolution diffusion-ordered spectroscopy (HR-DOSY)". Magnetic Resonance in Chemistry. 36 (10): 706–714. doi:10.1002/(SICI)1097-458X(199810)36:10<706::AID-OMR363>3.0.CO;2-W. S2CID   95455095.
  13. "Shoolery Award Recipient - SMASH - Small Molecule NMR Conference".