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Houston, TX, United States

William Marsh Rice University, commonly referred to as Rice University or Rice, is a private research university located on a 295-acre campus in Houston, Texas, United States. The university is situated near the Houston Museum District and is adjacent to the Texas Medical Center. It is consistently ranked among the top 20 universities in the U.S. and the top 100 in the world.Opened in 1912 after the murder of its namesake William Marsh Rice, Rice is now a research university with an undergraduate focus. Its emphasis on education is demonstrated by a small student body and 5:1 student-faculty ratio, among the lowest in the top American universities including the Ivy League. The university has produced 101 Fulbright Scholars, 11 Truman Scholars, 24 Marshall Scholars, 12 Rhodes Scholars, 3 Nobel Laureates, 2 Pulitzer Prize winners, and at least 2 deceased and 2 living billionaires. The university has a very high level of research activity for its size, with $115.3 million in sponsored research funding in 2011. Rice is noted for its applied science programs in the fields of artificial heart research, structural chemical analysis, signal processing, space science, and nanotechnology. It was ranked first in the world in materials science research by the Times Higher Education in 2010. Rice is a member of the Association of American Universities.Rice is noted for its entrepreneurial activity, and has been recognized as the top ranked business incubator in the world by the Stockholm-based UBI Index for both 2013 and 2014.The university is organized into eleven residential colleges and eight schools of academic study, including the Wiess School of Natural science, the George R. Brown School of Engineering, the School of Social science, and the School of Humanities. Graduate programs are offered through the Jesse H. Jones Graduate School of Business, School of Architecture, Shepherd School of Music, and Susanne M. Glasscock School of Continuing Studies. Rice students are bound by the strict Honor Code, which is enforced by a uniquely student-run Honor Council.Rice competes in 14 NCAA Division I varsity sports and is a part of Conference USA, often competing with its cross-town rival the University of Houston. Intramural and club sports are offered in a wide variety of activities such as jiu jitsu, water polo, and crew. Wikipedia.

Dai P.,Rice University
Reviews of Modern Physics | Year: 2015

High-transition temperature (high-Tc) superconductivity in the iron pnictides or chalcogenides emerges from the suppression of the static antiferromagnetic order in their parent compounds, similar to copper oxide superconductors. This raises a fundamental question concerning the role of magnetism in the superconductivity of these materials. Neutron scattering, a powerful probe to study the magnetic order and spin dynamics, plays an essential role in determining the relationship between magnetism and superconductivity in high-Tc superconductors. The rapid development of modern neutron time-of-flight spectrometers allows a direct determination of the spin dynamical properties of iron-based superconductors throughout the entire Brillouin zone. In this paper, an overview is presented of the neutron scattering results on iron-based superconductors, focusing on the evolution of spin-excitation spectra as a function of electron and hole doping and isoelectronic substitution. Spin dynamical properties of iron-based superconductors are compared with those of copper oxide and heavy fermion superconductors and the common features of spin excitations in these three families of unconventional superconductors and their relationship with superconductivity are discussed. © 2015 American Physical Society. Source

Ball Z.T.,Rice University
Accounts of Chemical Research | Year: 2013

Chemists have long been fascinated by metalloenzymes and their chemistry. Because enzymes are essential for biological processes and to life itself, they present a key to understanding the world around us. At the same time, if chemists could harness the reactivity and selectivity of enzymes in designed transition-metal catalysts, we would have access to a powerful practical advance in chemistry. But the design of enzyme-like catalysts from scratch presents enormous challenges. Simplified, designed systems often don't provide the opportunity to mimic the complex features of enzymes such as selectivity in polyfunctional environments and access to reactive intermediates incompatible with bulk aqueous solution.Extensive efforts by numerous groups have led to remarkable designed metalloproteins that contain complex folds, including well-defined secondary and tertiary structure surrounding complex polymetallic centers. These structural achievements, however, have not yet led to general approaches to useful catalysts; continued efforts and new insights are needed. Our efforts have combined the attributes of enzymatic and traditional catalysis, bringing the benefits of polypeptide ligands to bear on completely nonbiological transition-metal centers. With a focus on designing useful catalytic activity, we have examined rhodium(II) carboxylates, bound to peptide chains through carboxylate side chains. Among other advantages, these complexes are stable and catalytically active in water.Our efforts have centered on two main interests: (1) understanding how Nature's ligand of choice, polypeptides, can be used to control the chemistry of nonbiological metal centers, and (2) mimicking metalloenzyme characteristics in designed, nonbiological catalysts. This Account conveys our motivation and goals for these studies, outlines progress to date, and discusses the future of enzyme-like catalyst design.In particular, these studies have resulted in on-bead, high-throughput screens for asymmetric metallopeptide catalysts. In addition, peptide-based molecular recognition strategies have facilitated the site-specific modification of protein substrates. Molecular recognition enables site-specific, proximity-driven modification of a broad range of amino acids, and the concepts outlined here are compatible with natural protein substrates and with complex, cell-like environments. We have also explored rhodium metallopeptides as hybrid organic-inorganic inhibitor molecules that block protein-protein interactions. © 2012 American Chemical Society. Source

A method and system that provides a first nanoscale moiety with a first functionality and a second nanoscale moiety with a second functionality. The method system mixes the first and second nanoscale moieties and applies pressure to the mixture of the first and second nanoscale moieties for a period of time. The applied pressure causes the first and second functionalities to react to generate a product.

A magnetic resonance imaging enhancement agent includes a plurality of particles. Each particle including a metal core; a dielectric shell disposed on the metal core including water and at least one MRI contrast agent; and a metal shell disposed on the exterior surface of the dielectric shell that encapsulates the dielectric shell.

Rice University and Technology Holding, LLC | Date: 2015-10-22

The disclosure relates to biological methods of making a hydrocarbon feedstock wherein one-carbon substrates are converted into useful chemicals and fuels. Particularly, genetically engineered bacteria are used to make C4-C10 fatty acids or derivatives from one-carbon substrates such as methanol and carbon dioxide.

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