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American Chemical Society
Chemical Society of Washington, CSW

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The Hillebrand Prize

The Hillebrand Prize has been given annually since 1925 (except in 1929 and 1976) to a member or members of the Chemical Society of Washington for original contributions to the science of chemistry.

Hillebrand History and Past Recipients

 

Hillebrand Prize Nominations Due October 1st

Nominations for the 2007 Hillebrand Prize, CSW's most prestigious award, are due October 1st. Nominations have been solicited from local chemistry departments and Washington Metropolitan area laboratories, but any current member of CSW is eligible to make a nomination.

The Hillebrand Prize recognizes original contributions to science by one or more CSW members and carries a stipend of $2,000. The nomination package should contain a CV and a list of publications and should describe in some detail the research that forms the basis for the nomination. For further details, consult the CSW office, csw@acs.org


 

 

2007 Hillebrand Award Recipient

Ira W. Levin
Laboratory of Chemical Physics
National Institute of Diabetes and Digestive and Kidney Diseases
National Institutes of Health
Bethesda. Maryland 20892

Photo of Ira W. Levin, CSW Hillebrand Award winner for 2007

Dr. Levin received his B.S. from the University of Virginia and his Ph.D. from Brown University, as well as having engaged in postdoctoral experience at the University of Washington and having served a tour in the military. Having spent his professional career at the National Institutes of Health, he is currently Deputy Director of the Division of Intramural Research in the National Institute of Diabetes and Digestive and Kidney Diseases, in addition to being Chief, of the Section on Molecular Biophysics, at the NIH campus in Bethesda, Maryland. His research interests lie primarily in the applications of vibrational infrared and Raman spectroscopic techniques toward the elucidation of the conformational, dynamical, thermodynamic, and functional properties of both intact and model membrane assemblies and related systems. Emphasis is placed on investigating the specific lipid-lipid and lipid-protein interactions governing biomembrane reorganizations. In particular, his efforts are directed toward defining and characterizing lipid microdomain formation as it pertains both to the existence of lateral heterogeneities and transverse asymmetries within biological membranes and to the ability and extent of these fluctuating microclusters, or domain motifs, to modulate integral membrane protein behavior. He has been at the forefront of developing spectroscopic infrared, Raman and visible reflectance imaging instrumentation. Specifically, his laboratory has provided pioneering technologies and studies in spectroscopic Fourier-transform infrared and Raman microimaging. Current efforts are in actively translating laboratory imaging research into clinical venues ranging from monitoring disease progression by means of spectroscopic histopathologic classifications to in vivo hyperspectral visible reflectance imaging for assessing tissue perfusion, vascular disease and endothelial dysfunction.

Dr. Levin has been internationally recognized for his spectroscopic accomplishments and has been honored with many awards, including the Bomem-Michelson Award by the Coblentz Society, the Meggers Award (three separate award occasions) presented by the Society for Applied Spectroscopy, the distinguished Harold A. Iddles Lecture Series sponsored by the University of New Hampshire, and is a Fellow of the American Physical Society's Biophysical Division and, separately, a Fellow in the their Division of Chemical Physics. He has also received the Lippincott Award in Vibrational Spectroscopy presented by the Optical Society of America. Dr. Levin is a Fellow of the Society for Applied Spectroscopy and has received Honorary Membership in the Society, their highest award, for his pioneering technologies and studies in spectroscopic Fourier transform infrared and Raman microimaging. Dr. Levin has also received the New York Section of the Society for Applied Spectroscopy Gold Medal Award for his spectroscopic research contributions. He has served on numerous editorial and foundation advisory boards and committees in various leadership capacities, has lectured extensively, and has authored and coauthored approximately two hundred and thirty publications, in addition to several patents, over the course of his career. Dr. Levin is a member of the American Chemical Society, the American Physical Society, the American Society for Biochemistry and Molecular Biology, the Biophysical Society, the Coblentz Society, and the Society for Applied Spectroscopy.

Biomedical Applications of Infrared and Visible Reflectance
Spectroscopic Imaging: From Bench to Bedside

The blurring between the margins of disease detection and treatment has been termed the "science of prevention" by health practitioners. Major developments in this context have been within the exploding area of medical diagnostic imaging. A relatively recent contributor to the existing panoply of biomedical imaging techniques has been the applications of both vibrational spectroscopic and visible reflectance imaging approaches at the tissue level. These specific spectroscopic imaging techniques are capable of providing non-invasive characterizations of heterogeneous systems ranging from macromolecular assemblies to biological ensembles. Fourier transform infrared spectroscopic imaging, in particular, couples mid-infrared step-scan and continuous-scan interferometry both to infrared microscopes and appropriate infrared focal plane array and linear array detectors; this instrumentation has allowed enormous advances to be achieved in monitoring disease progression by means of histopathologic classifications. In combining the imaging of tissue microarrays with statistical pattern recognition algorithms, automated histologic segmentation based upon carefully specified spectral metrics is accomplished. These procedures preclude the use of tissue staining measures, are objective and statistically significant, and remain consonant with conventional tissue processing procedures. We will discuss here our recent developments in designing a practical imaging protocol for spectroscopically determining histopathologic features of, for example, prostate tissue. This process combines high throughput spectroscopic imaging, large scale patient sampling using tissue microarrays and rapid data analyses. As a further example of "translational research" (or bench to bedside research) in which a laboratory developed methodology is rapidly applied to clinical usage, we shall describe a non-invasive, visible reflectance hyperspectral technique for in vivo monitoring of vascular disease and endothelial dysfunction. This imaging approach has the potential for monitoring broad aspects of tissue perfusion in which vascular functional changes in human subjects are induced pharmacologically. Specifically, skin tissue hemoglobin oxygen saturation is imaged quantitatively in patients with sickle cell disease to determine whether changes in blood flow during nitric oxide stimulation or gas administration (therapies proposed for this disease) improve impaired tissue perfusion. In extending these concepts, we demonstrate an approach for visually enhancing, in real time, visible light images detected by a 3-CCD detector during laparoscopic procedures in which changes in tissue oxygenation become critical in surgical usage for the assessment of internal organ viability.

 

 

2006 Hillebrand Award Recipient

Robert Tycko


Photo of the Presentation of the 2006 Hillebrand Award to Dr. Robert Tycko by Dr. Becker and Dr. Stief at the CSW March 2007 Meeting
Presentation of the 2006 Hillebrand Award to Dr. Robert Tycko at the CSW March 2007 Meeting
Dr. Louis Stief, Dr. Ted Becker, Dr. Robert Tycko



Photo of Dr. Robert Tycko Robert Tycko received his A.B. from Princeton University in 1980, and his Ph.D. in chemistry from the University of California at Berkeley in 1984. After postdoctoral research at the University of Pennsylvania, he became a Member of Technical Staff in the Physical Chemistry Research Department of AT&T Bell Laboratories. At Bell Labs, Tycko worked on novel physical effects and experimental techniques in magnetic resonance spectroscopy, including effects of Berry's phase on spectra of rotating samples and techniques for zero field NMR in high field. He also carried out NMR studies that elucidated the molecular dynamics and electronic properties of fullerenes and superconducting alkali fullerides. Using optically-pumped NMR measurements on gallium arsenide quantum wells, Tycko obtained the first experimental evidence for skyrmion excitations in two-dimensional electron systems.

In 1994, Tycko joined the Laboratory of Chemical Physics of the National Institutes of Health. At the NIH, he has made numerous contributions to solid state NMR methodology for structural studies of proteins and other complex molecular systems. A major project in recent years has been the elucidation of the molecular structures of amyloid fibrils that are associated with Alzheimer's disease and related phenomena. Other current projects include applications of solid state NMR in investigations of protein folding and in structural studies of HIV-1 proteins.

 

Molecular Structure of Amyloid Fibrils (Why I Like Solid State NMR)

Robert Tycko
Laboratory of Chemical Physics
National Institute of Diabetes and Digestive and Kidney Diseases
National Institutes of Health, Bethesda, MD

Amyloid fibrils are self-assembled filamentous structures formed by a large class of polypeptides, including those associated with Alzheimer's disease, type 2 diabetes, Parkinson's disease, and transmissible spongiform encephalopathies. Because amyloid fibrils are inherently noncrystalline and insoluble, the molecular-level details of amyloid structures have been difficult to determine. Fortunately, amyloid fibrils are ideal systems for study by modern solid state NMR techniques. In his lecture on March 15th, Dr. Tycko will briefly introduce the ways in which solid state NMR measurements can provide structural constraints on amyloid fibrils. He will describe specific results, including full structural models for fibrils formed by the 40-residue β-amyloid peptide associated with Alzheimer's disease and preliminary models for fibrils associated with type 2 diabetes and yeast prions.

In the course of his lecture, Tycko will convey some of the characteristics of solid state NMR that have made it an interesting field of research for me over the past 25 years. These characteristics include fascinating mathematical theory of a type that is seldom encountered in other areas of chemistry and spectroscopy, as well as applicability to scientific problems that range from pure solid state physics to medically-relevant structural biology.

 

 

2005 Hillebrand Prize Recipient
Dr. Carter T. White

Photo of Dr. Carter T. White, 2005 Hillebrand Awardee and Speaker for the March 2006 CSW Meeting
Dr. Carter T. White, a native Virginian, received a BS from VA Tech in 1971 and a PhD from UVA in 1976. After a National Research Council Associateship with the Electronics Technology Division at the Naval Research Laboratory (NRL) he joined the NRL Chemistry Division staff in 1979 to work on electroactive polymers. At the time conventional wisdom held that an intrinsically conducting molecular wire was unlikely, if not impossible, because a spontaneous symmetry breaking would convert it into a semiconductor. However, in 1992 Dr. White and his coworkers, in the earliest published paper devoted to single-wall carbon nanotubes, predicted that armchair carbon nanotubes, if made, would overcome this roadblock as was experimentally confirmed years later. In a different area, his research group was the first to establish that large-scale molecular dynamics simulations could be used to directly link discrete atomic-scale chemistry to the continuum theory of condensedphase detonations. Over his career, Dr. White built the NRL Theoretical Chemistry Section from scratch and rose through the NRL ranks to become a Senior Scientist. He has also spent a year as a Program Director for Condensed Matter Theory at NSF (1985), as a Visiting Scientist within the Department of Materials at the University of Oxford (1996), and as Professor of Physics and Westinghouse Distinguished Professor of Materials Science and Engineering at Washington State University (1999). Because of his research on shock-induced chemistry, he has long been involved with the American Physical Society (APS) Topical Group on the Shock Compression of Condensed Matter most recently serving as Co-chair of the 14th APS Conference on Shock Compression Condensed Matter (2005). His research has been recognized by a number of awards including NRL's E. O. Hulburt Award (2005) and the Edison Chapter Sigma Xi Award for Pure Science (1996). Dr. White's publication list contains over 170 refereed papers with 7 of these receiving NRL Alan Berman Basic Research Publication Awards. In addition to being a member of the CSW, the ACS, and the MRS, Dr. White is a fellow of the APS through the Division of Chemical Physics.

 

Abstract

Working at the Interface between Chemistry and Allied Sciences
in Designing Metallic Polymers and Safer Explosives*

Carter T. White, Ph.D.

At the intersection of fullerenes, carbon fibers, and conducting polymers, singlewall armchair carbon nanotubes represent a novel class of low-dimensional materials with exceptional electronic properties. I will outline how we combined concepts from chemistry, polymers, and condensed matter physics to predict these remarkable properties which were confirmed experimentally years later following the successful synthesis of these tubes. The properties that make metallic armchair nanotubes so special will be described in basic terms and the strong interplay between theory and experiment that the rapidly growing field of nanotube research has enjoyed will be discussed. In a different area, I will briefly describe how we combined concepts from chemistry, materials science, and dynamics with large-scale molecular dynamics simulations to develop simplified models directly linking discrete atomic-scale chemistry to the theory of compressive reactive flows and how these models have recently begun to yield new insight into the design of safer condensed-phase explosives.

* Research Supported by the Office of Naval Research both directly and through the Naval Research Laboratory.

 

 

2004 Hillenbrand Prize Recipient
Dr. Catherine Fenselau

Photo of Dr. Catherine Fenselau Dr. Catherine Fenselau grew up in Nebraska, received her A.B. degree from Bryn Mawr College in Pennsylvania and her Ph.D. from Stanford University in the laboratory of Carl Djerassi. After post-doctoral work with Melvin Calvin and A.L. Burlingame at the University of California and the NASA Space Science Laboratory at Berkeley, she joined the faculty of Johns Hopkins University's Medical School. She rose through the ranks to become Professor there in 1982, and is Professor and Past Chair of the Department of Chemistry and Biochemistry at the University of Maryland. She is frequently invited to lecture in Europe, Asia and South America, and has been visiting professor at the University of Warwick and at Kansai Medical University. She was President of the American Society for Mass Spectrometry, founding Editor-in-Chief of Biomedical and Environmental Mass Spectrometry (1973-1989), and recipient of the Garvan Medal (1985), the Maryland Chemist award (1989) from the American Chemical Society, the Pittsburgh Spectroscopy Society Award (1993) and the 1999 Eastern Analytical Symposium award for Analytical Chemistry. Presently she is an Associate Editor for Analytical Chemistry and on the Board of Directors of the Maryland Science Center. Her research addresses biological mass spectrometry, proteomics, and the chemistry of conjugated drug metabolites. She has published more than 290 papers and book chapters and trained 140 students and post-doctoral fellows.

 

Abstract

Rapid Analysis of Microorganisms by Mass Spectrometry

Dr. Catherine Fenselau
University of Marland

The 2005 Hillebrand prize is awarded to Catherine Fenselau for the development of rapid biodetection methods based on mass spectrometry and bioinformatics. Such advanced systems will facilitate rapid medical diagnosis, monitoring and control of the spread of highly contagions diseases, and on time (detect to protect) recognition and identification of biohazards, particularly those associated with terrorism.

While it is now accepted by many that mass spectrometry provides a rapid and reliable method for detection and identification of biological agents, Anhalt and Fenselau in 1975 were the first to report that pathogenic bacteria could be introduced directly and intact into a mass spectrometer and that specific biomarkers could be vaporized, ionized and structurally identified. Most importantly, they demonstrated that the compositions and abundances of these chemical biomarkers, revealed in the mass spectra, allowed taxonomic distinctions to be made. Though the biomarkers observed in this early demonstration were small metabolites, the philosophy to employ intact biomarkers for rapid characterization of microorganisms by mass spectrometry was in clear contrast to all previous research, which had advocated vigorous pyrolysis prior to MS analysis. The biomarker concept has become the basis for all current applications of mass spectrometry for rapid detection and characterization of microorganisms. At least eight companies have launched commercial products designed to facilitate applications in food safety, medical diagnosis and homeland security. Most of this talk will address analyses made in the "detect to protect" time-frame.

The talk will review the capabilities of matrix assisted laser desorption (MALDI) mass spectrometry for rapid analysis of airborne microorganisms. Reproducibility of such spectra is difficult to control, depending on the laser power, matrix: sample ratio, conditions of growth and harvesting of the sample. The speaker's team has advocated the use of bioinformatics to relate a spectrum to a species of microorganism. This approach, which evolves from global progress in sequencing prokaryote genomes, can be implemented in several ways. In the approach that requires the simplest instrumental system, the masses of all proteins predicted by many genomes are calculated and compared to the protein masses observed by mass spectrometry. The significance of the match of this cohort to a particular bacterial/spore genome (species) is calculated, allowing for the sizes of the various genomes and accommodating common post-translational modifications. In another approach, applicable to toxins, viruses and species with small sets of proteins, the protein can be cleaved chemically or enzymatically in the sample holder, and masses of the parent protein as well as masses of the polypeptide cleavage products can be matched against sets of masses predicted in silico. In a third approach, applicable to mixtures of microorganisms, limited numbers of proteins are released from the cell by selective chemistry and incubated in situ with proteolytic enzymes. As many peptides as possible are rapidly analyzed by tandem mass spectrometry to provide partial sequences of each. These microsequences provide reliable identifications, searched against known protein sequences, of proteins and thereby of genus and species in the mixture.

One of the great strengths of mass spectrometry is that the analyst is not limited to monitoring pre-selected target species. The mass spectrometer provides broad band information on whatever is there. However, detection speed and sensitivity can be enhanced by identifying peptides that are unique to organisms of concern, for example anthrax.

 

 

2003 Hillebrand Prize Recipient
Dr. Kenneth A. Jacobson

Photgraph of Dr. Kenneth A. Jacobson Kenneth A. Jacobson is Chief of the Molecular Recognition Section (1993 - present), and in 2003 was appointed as the first Director of the new Chemical Biology Core Facility, both at the National Institute of Diabetes, Digestive, and Kidney Diseases, of the National Institutes of Health in Bethesda, MD. The Chemical Biology Core Facility forms the interface between biological and chemical laboratories in the Institute, adding its expertise as needed, either in organic synthesis or in the pharmacological area. He also is an Adjunct Professor at the Uniformed Services University of the Health Sciences, Bethesda, MD, in the Department of Anatomy, Physiology, and Genetics.

Dr. Jacobson is a medicinal chemist with interests in the structure and pharmacology of G protein-coupled receptors; in particular, receptors for adenosine and nucleotides such as adenosine 5'-triphosphate (ATP). He has taken an interdisciplinary approach involving synthesis and the in-depth study of both the ligands (i.e., small molecules), which are potential therapeutic agents, and their protein targets (i.e., receptors). His group was the first to model adenosine and ATP receptors based on a rhodopsin template, and in 1996, they introduced the first on-line database of receptor mutagenesis. He was the first to introduce selective, high affinity agonists or antagonists of the A1, A2B, and A3 adenosine receptors and P2Y1 nucleotide receptors, which are used universally as pharmacological research tools. Ken has developed a "functionalized congener approach" to drug design. His approach to ligand development and receptor modeling of A3 adenosine receptors was featured as the cover story in C and E News (February 12, 2001). He developed a general methodology for radiofluorination for in vivo positron emission tomography (PET scanning) of peptide receptors, such as insulin receptors. Recently, Dr. Jacobson introduced a general approach to engineered G protein-coupled receptors, termed "neoceptors". Ken is involved in the basic science leading to drug discovery for new treatment of asthma, cystic fibrosis, cardiac ischemia, thrombosis, stroke, and neurodegenerative diseases. His collaboration with Dr. Bruce Liang (of the Univ. of Connecticut) on the development of new cardioprotective agents was featured in USA Today (see: http://www.eurekalert.org/releases/upmc-newtis.html ).

Ken Jacobson received his B.A. degree (1976) from Reed College, and M.S. (1978) and Ph.D. degrees in Chemistry (1981) with Prof. Murray Goodman at the University of California, San Diego. He was Bantrell Postdoctoral Fellow with Prof. A. Patchornik in the Dept. of Organic Chemistry, Weizmann Institute, before joining the NIH in 1983. He has authored or co-authored 350 original research papers, edited three books, and is listed as inventor on 40 patents. He has trained dozens of postdoctoral fellows from many countries. Ken has served on the editorial advisory boards of the Jour. of Medicinal Chemistry, Bioconjugate Chemistry, Drug Development Research, Drug Design and Discovery, Expert Opinion on Therapeutic Patents, Current Topics in Medicinal Chemistry, and Medicinal Research Reviews. He has initiated formal collaborative research projects between NIH and the pharmaceutical industry. Ken also has been a consultant to private industry. Dr. Jacobson has been a member of the ACS since 1980, and in 2004 was elected to serve at the national level, as Chair of the Medicinal Chemistry Division. He has planned and directed ACS symposia on: P2 nucleotide receptors, cyclin-dependent kinases, cannabinoids, adenosine receptors, allosteric modulation of G protein-coupled receptors, and engineered G protein-coupled receptors. He is also a member of the Society for Neuroscience, the American Society for Pharmacology and Experimental Therapeutics (FASEB), International Society for Nucleosides, Nucleotides and Nucleic Acids, the International Purine Club (serves as representative of the U. S.), and the IUPHAR Committees on Nomenclature of Adenosine and P2Y Receptors. In 1996 Ken was recognized by the International Purine Club as the first recipient of the Fassina Award for "his many and varied contributions to the field of purinergic research by providing important and novel chemical probes", and in 2001 was awarded the Roon Lectureship at Scripps Research Inst., La Jolla, CA. He was awarded the designation of "Highly Cited Researcher" (among the 200 most highly cited pharmacologists worldwide) by the Institute for Scientific Information.

 

Abstract

Perspective of an NIH Chemist on Purine-Based
Treatment of Ischemia of the Heart and Brain

Dr. Kenneth A. Jacobson
Laboratory of Bioorganic Chemistry, NIDDK

Extracelluar adenosine, purine nucleotides (such as ATP and ADP), and pyrimidine nucleotides (such as UTP and UDP) act as neurotransmitters/ neuromodulators. These ubiquitous signaling molecules modulate the function of diverse mammalian cell types and tissues under both normal and pathophysiological conditions. We have characterized receptors for extracellular nucleosides and nucleotides through medicinal chemical, molecular biological, and pharmacological approaches.

Adenosine is involved in many of the body's cytoprotective functions, including protecting cardiac muscle cells and neurons in the brain against the damaging effects of ischemia. Four subtypes of adenosine receptors (ARs), termed A1, A2A, A2B and A3 (all of which are heptahelical G protein-coupled receptors) have been defined. We have designed the first protypical, selective agonists and antagonists for the A3AR and other subtypes. We explored the structure-functional analysis of the receptors, as well as structure-activity relationships (SAR) of their ligands. We have used mutagenesis and computer modeling to generate knowledge of the three dimensional structure of the purine receptors and their mechanism of activation in order to design novel agonists and antagonists. We discovered the cardioprotective and cerebroprotective properties of selective A3AR agonists, demonstrated in both cellular and animal models. We have shown that chronic treatment in gerbils with the first prototypical A3AR agonist, IB-MECA*, protects hippocampal neurons, and improves the cognitive performance following global ischemia. The more potent and selective CI-IB-MECA protects cardiac myocytes when administered either before or during prolonged ischemia. Due to its cytostatic effects on tumor growth, IB-MECA is currently in clinical trials for use in treating colon carcinoma and melanoma. Another potential means of using the protective effects of AR activation was achieved through an approach to receptor engineering introduced in our laboratory. By this approach of "neoceptors", intended for eventual gene therapy, the putative agonist binding site on the receptor is redesigned to accept only agonist molecules altered in a complementary fashion.
(* IB-MECA is N 6-(3-iodobenzyl)-5'-N-methylcarboxamidoadenosine).

The nucleoside adenosine and the nucleotides ADP and ATP are related metabolically, but they act at distinct receptors. Eight subtypes of P2Y nucleotide receptors have been defined. Among the many therapeutic interests related to these receptors is antiplatelet therapy. The stimulation of both P2Y1 and P2Y12 receptors by ADP, produced during vascular injury, is an important proaggregatory signal in platelets. Thus, selective antagonists for these receptors are of interest in the prevention of thrombus, which can result in heart attack and stroke. Through extensive SAR studies of synthetic nucleotides, we have developed the first high affinity and selective antagonists of the P2Y1 receptor.

We have recently focused on conformational factors of the ribose or ribose-like moiety. We found that a constrained carbocyclic ring system locked in the Northern (N) envelope conformation is preferred for both agonists and antagonists over other conformations in P2Y1 receptor binding. Based on this principal, we have introduced MRS2500, which is the most potent known antagonist of the P2Y1 receptor, and effectively inhibits platelet aggregation.

 

 

2002 Hillebrand Award Recipient

Dr. Russell J. Hemley

Photgraph of Dr. Russell J. Hemley Russell J. Hemley's research explores the chemistry of materials over a broad range of thermodynamic conditions from low to very high pressures. He began his research career in molecular spectroscopy and electronic structure theory. An interest in the effects of high pressures on materials led him to the Geophysical Laboratory of the Carnegie Institution of Washington. There he began to apply and extend chemical physics techniques in high-pressure diamond anvil cell experiments. Since then, his research program has expanded to include high-pressure experimental and theoretical studies in condensed matter physics, earth and planetary science, and materials science. Some of his accomplishments include the discovery of new phenomena in dense hydrogen at megabar pressures; observations of unusual transformations in molecular materials and novel high-pressure molecular compounds; the creation of new superconductors, magnetic structures, glasses, and superhard materials under pressure. He is also involved in the continued development of high-pressure techniques, including optical methods, synchrotron radiation for diffraction and spectroscopy, and transport measurements.

Russell J. Hemley grew up in California, Colorado, and Utah, and attended Wesleyan University, where he studied chemistry and philosophy (B.A., 1977). He did his graduate work in physical chemistry at Harvard University (M.A., 1980; Ph.D. 1983). After a post-doctoral fellowship in theoretical chemistry at Harvard (1983-84), he joined the Geophysical Laboratory as a Carnegie Fellow (1984-86) and Research Associate (1986-87), and became a Staff Scientist in 1987. He has been a visiting Professor at the Johns Hopkins University (1991-92) and at the Ecole Normale Supérieure, Lyon (1996). He is the recipient of the 1990 Mineralogical Society of America Award, and is a Fellow of the American Physical Society, the American Geophysical Union, and the American Academy of Arts and Sciences. He was elected as a member of the National Academy of Sciences in 2001. He has published approximately 320 scientific articles and has edited four books.

 

Abstract

The New Chemistry of Materials Under Pressure

Russell J. Hemley, Ph.D.

Historically, chemistry has fully utilized only two of its three fundamental tools -- the variables of composition and temperature. Pressure, the third principal thermodynamic variable, is in many ways the most remarkable, as it spans some 60 orders of magnitude in the universe. Yet, until recently its use in the laboratory has been quite restricted. With recent advances in techniques to generate very high pressures, materials can be subjected to, and observed at, millions of atmospheres pressures. Materials can also be heated to thousands of degrees or cooled to millikelvin temperatures while at these extreme pressures, and examined using a wide variety of new techniques including intense laser, synchrotron x-ray, and spallation neutron methods.

These experiments reveal a "brave, new world" of chemistry under extreme pressures. The field is providing fertile ground for the formation of new materials, greatly expanding the number of known substances. More significantly, entirely new classes of materials are appearing. New forms of common and putatively simple substances such as hydrogen, nitrogen, and water (and their mixtures) occur when compressed. Other gases and liquids are not only solidified under pressures but can be turned into metals and even superconductors. Both the highest temperature superconductivity on record (164° K) and new kinds of superconductors have been produced. Chemical bonds and affinities of otherwise familiar elements and compounds are totally changed. "Inert" gases form compounds; normally unreactive metals form new alloys. The common silicate and oxide minerals found near the Earth's surface transform to dense, strong ceramic substances that are now believed to make up the bulk of our planet. Even at more modest pressures of several thousand atmospheres, strong effects on organic and biochemical reactions are observed. In effect, the variable of pressure is adding a new dimension to the venerable Periodic Table. The implications span the physical and even biological sciences.

 

 

The Supreme Court of Chemistry

by Lisa Greenhouse, NIST Historian

The annual Hillebrand Prize of the Chemical Society of Washington (CSW), awarded for original contributions to the science of chemistry by member(s) of CSW, is named for William F. Hillebrand (1853-1925), one of Washington's most distinguished chemists. Hillebrand achieved such stature during his career in Washington, first with the Geological Survey and then with the Bureau of Standards, that his colleagues referred to him as the "Supreme Court of Chemistry."

Hillebrand was indeed a judge and a critic but a reluctant one. As Chairman for many years of the Supervisory Committee on Standard Methods of Analysis of the American Chemical Society (ACS), he played a paramount role in judging which analytical methods would be published as ACS standards. As associate editor of the Journal of the American Chemical Society and assistant editor of Chemical Abstracts and the Journal of Industrial and Engineering Chemistry, the latter of which he founded, Hillebrand placed himself in the delicate position of having to critique and often reject the work of his professional peers. He performed these duties with great integrity but also with some unhappiness, never feeling good about disappointing his colleagues.

In several addresses to scientific societies, Hillebrand was sharply critical of what was then the growing tendency of his profession to make incomplete chemical analyses of samples, leaving out elements present in small amounts and leaving out determinations of rare elements that were thought not to be useful. This was so even when important uses for rare elements continued to be discovered. Hillebrand, an analytical geochemist by training, deplored this trend toward incompleteness and was outspoken in his criticism.

Hillebrand's conviction that analytical chemistry should be exacting was indicative of his perfectionism. More than a judge of others, he was a judge of himself. He always regretted that he had what he considered an inadequate grasp of mathematics and English composition, and he didn't fail to mention these deficiencies in autobiographical notes. He modestly referred to Thomas H. Norton, his classmate at the University of Heidelberg, where Hillebrand received his PhD, summa cum laude, in 1875, as having "superior mental power" to his own. He struggled with embarrassment over his failure to find terrestrial helium in a sample of uraninite, which he had analyzed in 1887, an error pointed up by Sir William Ramsay's later discovery of helium in a variety of uraninite.

After Heidelberg, Hillebrand studied at the Mining Academy at Freiberg, Germany. Thus prepared, Hillebrand returned to America to pursue a career as a geochemist. In 1880, after running a private assaying firm in Leadville, Colorado, a silver mining boomtown, he took a job as an analytical chemist with the U.S. Geological Survey's Denver laboratory. He was soon transferred to Washington where he made major contributions to the understanding of silicate rocks.

In 1908, Hillebrand moved to the Bureau of Standards (founded in 1901 as a national standards laboratory) as Chief Chemist. Hillebrand, with scant resources and a few staff members, set out on a groundbreaking path of preparing and providing well-characterized samples necessary for American industry to check its analytical methods, techniques, and instruments. The Standard Reference Materials Program that Hillebrand established continues to be one of the most significant missions of the National Institute of Standards and Technology.

 

Photo of William F. Hillebrand (1853-1925)

Dr. William F. Hillebrand

YEAR  RECIPIENT(S)
2007Ira W. Levin
2006Robert Tycko
2005Carter T. White
2004Catherine Fenselau
2003Kenneth A. Jacobson
2002Russell J. Hemley
2001Louis J. Stief
2000Akbar Montaser
1999Michael T. Pope
1998Ad Bax
James A. Ferretti
1997Derek Horton
1996William A. Eaton
H. James Hofrichter
1995Millard H. Alexander
1994Edith Wilson Miles
1993Frances S. Ligler
1992Richard J. Colton
1991Seymour Kaufman
1990Marilyn E. Jacox
1989Miral Dizdaroglu
1988David E. Ramaker
1987N. Bhushan Mandava
Malcolm J. Thompson
1986Celia W. Tabor
Herbert Tabor
1985Kenner C. Rice
1984Ying-Nan Chiu
1983William J. Bailey
1982Jimmie Reed McDonald
1981Alexander J. Fatiadi
1980Elizabeth K. Weisburger
1979Donald M. Jerina
1978James R. Griffith
Thressa C. Stadtman
1977John William Daly
1976[Award not accepted]
1975Ming Chang Lin
1974Elizabeth F. Neufeld
1973Daniel P. Schwartz
1972Frederick A. H. Rice
1971Nicolae Filipescu
1970Herbert A. Sober
Elbert A. Peterson
1969Isabella L. Karle
Jerome Karle
1968Earl R. Stadtman
1967Everette L. May
Nathan B. Eddy
1966Arthur A. Westenberg
Robert M. Fristrom
1965Marshall W. Nirenberg
1964Ellis R. Lippincott, Jr.
1963Martin Jacobson
Morton Beroza
1962Philip H. Abelson
1961Sidney Udenfried
1960Frank T. McClure
1959Leon A. Heppel
1958Bernhard Witkop
1957Jesse P. Greenstein
1956Francis O. Rice
1955Roger G. Bates
1954William A. Zisman
1953Bernard L. Horecker
1952Dean Burk
1951Horace S. Isbell
1950Henry Stevens
E. Jack Coulson
Joseph R. Spies
1949Lyndon F. Small
1948Edgar R. Smith
1947Nathan L. Drake
1946John I. Hoffman
1945Stephen Brunauer
1944Raymond M. Hann
1943Ben H. Nicolet
1942J. Frank Schairer
1941Michael X. Sullivan
1940Ferdinand G. Brickwedde
1939Ralph E. Gibson
1938Raleigh Gilchrist
Edward Wichers
1937Sterling B. Hendricks
1936Vincent Du Vigneaud
1935Oliver R. Wulf
1934Frederick D. Rossini
1933Edward Wight Washburn
1932F. B. La Forge
Herman L. J. Waller
1931Gustav F. Lundell
1930Claude S. Hudson
1929[No Award]
1928James H. Hibben
1927Edward P. Bartlett
1926George W. Morey
1925Richard Fay Jackson


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