Melinda Duer | |
---|---|
Born | Melinda J. Duer 1 October 1963 |
Nationality | British |
Education | University of Cambridge (BA, MA, PhD) |
Awards | Interdisciplinary Prize (2017) Suffrage Science award (2019) |
Scientific career | |
Fields | Biological chemistry and biomedical Chemistry |
Institutions | University of Cambridge Robinson College, Cambridge |
Thesis | The parametric probes of ligand field theory (1988) |
Doctoral advisor | Malcolm Gerloch |
Website | Duer Lab Robinson College webpage |
Melinda Jane Duer FRSC is Professor of Biological and Biomedical Chemistry in the Department of Chemistry at the University of Cambridge, and was the first woman to be appointed to an academic position in the department. Her research investigates changes in molecular structure of the extracellular matrix in tissues in disease and during ageing. She serves as Deputy Warden of Robinson College, Cambridge. [1] She is an editorial board member of the Journal of Magnetic Resonance. [2]
Duer attended Sir James Smith's School, a comprehensive school in North Cornwall. [3] [4] [5] She enjoyed science at high school and was encouraged by her chemistry teacher to study natural sciences at Emmanuel College, Cambridge, where she specialized in chemistry. [4] She was the first member of her family to attend higher education. [5] [6] Duer went on to complete her PhD in 1988 in theoretical chemistry with Malcolm Gerloch, where she investigated ligand field theory. [7]
During the course of her PhD research, Duer developed an interest in nuclear magnetic resonance spectroscopy (NMR) while chatting with Lynn Gladden who frequently worked on the spectrometer in the room opposite Duer's office at the time. Towards the end of her PhD, Duer proposed using solid-state NMR to investigate organometallic catalytic species in response to an advertised temporary lectureship in the department. [8] Thus, she became the first woman to be appointed to a lectureship in the Department of Chemistry at the University of Cambridge in 1988. [4] In 1990, she was awarded a Royal Society University Research Fellowship. [8] [9]
Duer begun her research in solid-state NMR by investigating molecular mobility in porous materials in collaboration with Gladden who has moved to the Department of Chemical Engineering. [10] [11] [12] She went on to investigate molecular mobility more broadly, in polymers and other solids. [8] [13] With a theoretical chemistry background and through discussions with Malcolm Levitt and others, Duer also developed solid-state NMR experiments to probe anisotropic interactions, such as quadrupolar interactions [14] [15] [16] [17] and chemical shift anisotropy. [18] [19] [20] In 2001 and 2004, she published two books on solid-state NMR, targeted at graduate students. [21] [22]
In early 2000s, Duer pioneered the use of solid-state NMR to investigate biological tissues, including keratin [23] and bones, [24] frequently obtained from horses due to her interest in horse riding. [3] Her previous research on liquid crystal phases of polymers led her to wonder whether similar phases could form in keratin. [4]
Duer has extensively investigated the extracellular matrix, the component of biological tissues that simultaneously serves as the communication system between cells and provides a scaffold to support them. She is particularly interested in the molecular mechanisms that underpin the functions of the extracellular matrix. By understanding the structure-property relationships of biological tissue, Duer works to unravel the processes that give rise to collagenous tissue and mineralisation. [25]
Duer has investigated the calcification of blood vessels that occurs when people age. [4] She proposed that the hardening of arteries caused by the build-up of calcium may be triggered by polymeric adenosine diphosphate ribose (PAR), a molecule that is produced when the DNA inside cells is damaged. [26] One of her graduate students launched a spin-out company, Cycle Pharmaceuticals, which provides personalised treatment to patients with vascular diseases. [4] She was promoted to Professor in 2015. [4]
Duer was awarded the Royal Society of Chemistry Interdisciplinary Prize in 2017, [27] and the Suffrage Science award in 2019. [28] [29]
Apart from licensing novel treatment for treating vascular disease to Cycle Pharmaceuticals, [30] [31] Duer is a co-founder of Cambridge Oncology Ltd. [32]
Duer is part of the Strategic Advisory Group of the Cambridge-Africa Programme, an initiative by the University of Cambridge to strengthen research capacity with African universities and research institutions. [33] In this role, Duer mentors African academics such as Dr Mercy Badu of Kwame Nkrumah University of Science and Technology. [34]
As a previous holder of the Suffrage Science award, Duer nominated Dr Mary Anti Chama of the University of Ghana for the same award in 2021. [35] [36] [37] [38]
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: CS1 maint: others (link)Duer used to be an equestrian, and has said that her interest in biological chemistry started with studying keratin in horses hooves and understanding leg fractures in one of her rescue horses. [4] [5] Her other interests include cycling and competing in triathlons.
Spectroscopy is the field of study that measures and interprets electromagnetic spectrum. In narrower contexts, spectroscopy is the precise study of color as generalized from visible light to all bands of the electromagnetic spectrum.
Nuclear magnetic resonance spectroscopy, most commonly known as NMR spectroscopy or magnetic resonance spectroscopy (MRS), is a spectroscopic technique based on re-orientation of atomic nuclei with non-zero nuclear spins in an external magnetic field. This re-orientation occurs with absorption of electromagnetic radiation in the radio frequency region from roughly 4 to 900 MHz, which depends on the isotopic nature of the nucleus and increased proportionally to the strength of the external magnetic field. Notably, the resonance frequency of each NMR-active nucleus depends on its chemical environment. As a result, NMR spectra provide information about individual functional groups present in the sample, as well as about connections between nearby nuclei in the same molecule. As the NMR spectra are unique or highly characteristic to individual compounds and functional groups, NMR spectroscopy is one of the most important methods to identify molecular structures, particularly of organic compounds.
In solid-state NMR spectroscopy, magic-angle spinning (MAS) is a technique routinely used to produce better resolution NMR spectra. MAS NMR consists in spinning the sample at the magic angle θm with respect to the direction of the magnetic field.
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.
The magic angle is a precisely defined angle, the value of which is approximately 54.7356°. The magic angle is a root of a second-order Legendre polynomial, P2(cos θ) = 0, and so any interaction which depends on this second-order Legendre polynomial vanishes at the magic angle. This property makes the magic angle of particular importance in magic angle spinning solid-state NMR spectroscopy. In magnetic resonance imaging, structures with ordered collagen, such as tendons and ligaments, oriented at the magic angle may appear hyperintense in some sequences; this is called the magic angle artifact or effect.
A Pake Doublet is a characteristic line shape seen in solid-state nuclear magnetic resonance and electron paramagnetic resonance spectroscopy. It was first described by George Pake.
In nuclear chemistry and nuclear physics, J-couplings are mediated through chemical bonds connecting two spins. It is an indirect interaction between two nuclear spins that arises from hyperfine interactions between the nuclei and local electrons. In NMR spectroscopy, J-coupling contains information about relative bond distances and angles. Most importantly, J-coupling provides information on the connectivity of chemical bonds. It is responsible for the often complex splitting of resonance lines in the NMR spectra of fairly simple molecules.
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.
Biophysical chemistry is a physical science that uses the concepts of physics and physical chemistry for the study of biological systems. The most common feature of the research in this subject is to seek an explanation of the various phenomena in biological systems in terms of either the molecules that make up the system or the supra-molecular structure of these systems. Apart from the biological applications, recent research showed progress in the medical field as well.
Nuclear magnetic resonance (NMR) is a physical phenomenon in which nuclei in a strong constant magnetic field are disturbed 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. High-resolution 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). The original application of NMR to condensed matter physics is nowadays mostly devoted to strongly correlated electron systems. It reveals large many-body couplings by fast broadband detection and should not be confused with solid state NMR, which aims at removing the effect of the same couplings by Magic Angle Spinning techniques.
Deuterium NMR is NMR spectroscopy of deuterium, an isotope of hydrogen. Deuterium is an isotope with spin = 1, unlike hydrogen-1, which has spin = 1/2. The term deuteron NMR, in direct analogy to proton NMR, is also used. Deuterium NMR has a range of chemical shift similar to proton NMR but with poor resolution, due to the smaller magnitude of the magnetic dipole moment of the deuteron relative to the proton. It may be used to verify the effectiveness of deuteration: a deuterated compound will show a strong peak in 2H NMR but not proton NMR.
Nuclear magnetic resonance crystallography is a method which utilizes primarily NMR spectroscopy to determine the structure of solid materials on the atomic scale. Thus, solid-state NMR spectroscopy would be used primarily, possibly supplemented by quantum chemistry calculations, powder diffraction etc. If suitable crystals can be grown, any crystallographic method would generally be preferred to determine the crystal structure comprising in case of organic compounds the molecular structures and molecular packing. The main interest in NMR crystallography is in microcrystalline materials which are amenable to this method but not to X-ray, neutron and electron diffraction. This is largely because interactions of comparably short range are measured in NMR crystallography.
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.
Structural chemistry is a part of chemistry and deals with spatial structures of molecules and solids. For structure elucidation a range of different methods is used. One has to distinguish between methods that elucidate solely the connectivity between atoms (constitution) and such that provide precise three dimensional information such as atom coordinates, bond lengths and angles and torsional angles.
Lucio Frydman is an Israeli chemist whose research focuses on magnetic resonance imaging (MRI), nuclear magnetic resonance (NMR) and solid-state NMR. He was awarded the 2000 Günther Laukien Prize, the 2013 Russell Varian Prize and the 2021 Ernst Prize. He is Professor and Head of the Department of Chemical and Biological Physics at the Weizmann Institute of Science in Israel and Chief Scientist in Chemistry and Biology at the US National High Magnetic Field Laboratory in Tallahassee, Florida. He is a fellow of the International Society of Magnetic Resonance and of the International Society of Magnetic Resonance in Medicine. He was the Editor-in-Chief of the Journal of Magnetic Resonance (2011-2021).
Mei Hong is a Chinese-American biophysical chemist and professor of chemistry at the Massachusetts Institute of Technology. She is known for her creative development and application of solid-state nuclear magnetic resonance (ssNMR) spectroscopy to elucidate the structures and mechanisms of membrane proteins, plant cell walls, and amyloid proteins. She has received a number of recognitions for her work, including the American Chemical Society Nakanishi Prize in 2021, Günther Laukien Prize in 2014, the Protein Society Young Investigator award in 2012, and the American Chemical Society’s Pure Chemistry award in 2003.
Jean Baum is an American chemist. She is the distinguished professor of chemistry and chemical biology at Rutgers University, where she is also vice dean for research and graduate education in the school of arts and sciences, and also vice chair of the department of chemistry and chemical biology. Her research investigates protein–protein interaction and protein aggregation using nuclear magnetic resonance spectroscopy (NMR) and other biochemical and biophysical techniques. She serves as treasurer for the Protein Society.
Alfred G. Redfield was an American physicist and biochemist. In 1955 he published the Redfield relaxation theory, effectively moving the practice of NMR or Nuclear magnetic resonance from the realm of classical physics to the realm of semiclassical physics. He continued to find novel magnetic resonance applications to solve real-world problems throughout his life.
Lucia Banci is an Italian chemist who is a professor at the University of Florence. Her research considers structural biology and biological nuclear magnetic resonance, with a focus on the role of metal ions in biological systems.
Eric Oldfield is a British chemist, the Harriet A. Harlin Professor of Chemistry and a professor of Biophysics at the University of Illinois at Urbana-Champaign. He is known for his work in nuclear magnetic resonance spectroscopy of lipids, proteins, and membranes; of inorganic solids; in computational chemistry, and in microbiology and parasitology. He has received a number of recognitions for his work, including the American Chemical Society's Award in Pure Chemistry, the Royal Society of Chemistry's Meldola Medal and the Biochemical Society's Colworth Medal, and he is a member of the American Association for the Advancement of Science, a Fellow of the Royal Society of Chemistry, and a Fellow of the American Physical Society.
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