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December 22, 2003
Volume 81, Number 51
CENEAR 81 51 pp. 39-50

ISSN 0009-2347



In structural biochemistry in late 2002, Lucio Frydman and coworkers at Weizmann Institute of Science, Rehovot, Israel, developed ultrafast multidimensional nuclear magnetic resonance (NMR) spectroscopy, which shortens by orders of magnitude the time required to obtain 2-D and 3-D NMR spectra [Proc. Natl. Acad. Sci. USA, 99, 15858 (2002)]. The technique could speed studies of chemical structure and dynamics. And this year a technique called G-matrix Fourier transform NMR was devised by Thomas Szyperski and postdoc Seho Kim of the State University of New York, Buffalo, also for the purpose of speeding multidimensional NMR [J. Am. Chem. Soc., 125, 1385 (2003)].


ELEVATOR Koshland and coworkers obtained the first structures of drugs complexed with a bacterial multidrug-transporter protein and proposed an "elevator" mechanism. COURTESY OF E. YU, H. NIKAIDO, & D. KOSHLAND

Using a 2-D NMR correlation approach, the first high-resolution NMR spectra of disordered solids--such as glasses, polymers, and biomaterials--were obtained by Lyndon Emsley of Ecole Normale Supérieure, Lyon, France; Alexander Pines at the University of California, Berkeley; and coworkers [J. Am. Chem. Soc., 125, 4376 (2003)].

Using X-ray crystallography and kinetics, Dan S. Tawfik of Weizmann Institute of Science and coworkers found that a single antibody can take on two different conformations, enabling it to bind two unrelated antigens [Science, 299, 1362 (2003)].

A group led by Daniel E. Koshland Jr. of the University of California, Berkeley, determined the first structures that show drugs complexed with a bacterial multidrug-transporter protein and proposed an "elevator" mechanism of action [Science, 300, 976 (2003)].

A structural and mechanistic study of a voltage-dependent potassium ion channel by Roderick MacKinnon of Rockefeller University, New York City, challenged a long-standing view about the mechanism by which this type of channel opens and closes in response to charge-distribution changes [Nature, 423, 33 and 42 (2003)]. MacKinnon shared the 2003 Nobel Prize in Chemistry with Peter Agre of Johns Hopkins University School of Medicine for research on cell membrane channels.

Two groups obtained high-resolution structures of previously elusive members of a family of membrane transporter proteins [Science, 301, 610 and 616 (2003)]. The structure of LacY was solved by a team led by H. Ronald Kaback of the University of California, Los Angeles, and So Iwata of Imperial College, London. And Da-Neng Wang and coworkers at New York University School of Medicine obtained the structure of GlpT.

Three independent teams determined the unusual structure of the antibacterial peptide microcin J25, one of the few known natural molecules that block bacterial RNA polymerase [J. Am. Chem. Soc., 125, 12382, 12464, and 12475 (2003)]. The studies were carried out by Gaetano T. Montelione of Rutgers University's Center for Advanced Biotechnology & Medicine and Richard H. Ebright of Howard Hughes Medical Institute and the Waksman Institute at Rutgers; David J. Craik at the University of Queensland, Brisbane, Australia; Seth A. Darst of Rockefeller University and coworkers.

Earlier this month, crystal structures of plant photosystem I (by Nathan Nelson of Tel Aviv University and coworkers) and the reaction center/light-harvesting 1 complex of purple bacteria (by Neil W. Isaacs, Richard J. Cogdell, and coworkers at the University of Glasgow) revealed previously unknown details about photosynthetic systems [Nature, 426, 630 (2003); Science, 302, 1969 (2003)].

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TRANSPORTERS Kaback, Iwata, and coworkers determined the structure of LacY (left), and Wang's group obtained that of GlpT. © SCIENCE 2003

Chemistry Highlights 2003
Organics & Carbs
Sensors & Analysis
Inorganic Chemistry
Supramolecular Chemistry
Nanotech & Molecular Electronics
Polymer Chemistry
Physical & Surface Chemistry


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