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  • 1
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    Determination of spin and orbital magnetization in the ferromagnetic superconductor UCoGe (2015)
    American Physical Society (APS)
    Details
    Publication Date: 2015-09-15
    Description: Author(s): M. W. Butchers, J. A. Duffy, J. W. Taylor, S. R. Giblin, S. B. Dugdale, C. Stock, P. H. Tobash, E. D. Bauer, and C. Paulsen The magnetism in the ferromagnetic superconductor UCoGe has been studied using a combination of magnetic Compton scattering, bulk magnetization, x-ray magnetic circular dichroism, and electronic structure calculations, in order to determine the spin and orbital moments. The experimentally observed t… [Phys. Rev. B 92, 121107(R)] Published Mon Sep 14, 2015
    Keywords: Electronic structure and strongly correlated systems
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
    Published by American Physical Society (APS)
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  • 2
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    Interstitial iron tuning of the spin fluctuations in the nonsuperconducting parent phase Fe_{1+x}Te (2011)
    American Physical Society (APS)
    Details
    Publication Date: 2011-07-19
    Description: Author(s): Chris Stock, Efrain E. Rodriguez, Mark A. Green, Peter Zavalij, and Jose A. Rodriguez-Rivera Using neutron inelastic scattering, we investigate the low-energy spin fluctuations in Fe 1+ x Te as a function of both temperature and interstitial iron concentration. For Fe 1.057(7) Te , the magnetic structure is defined by a commensurate wave vector of ( 1/2,0,1/2 ). The spin fluctuations are gapped wit... [Phys. Rev. B 84, 045124] Published Mon Jul 18, 2011
    Keywords: Electronic structure and strongly correlated systems
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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  • 3
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    Magnetic and structural properties near the Lifshitz point in Fe_{1+x}Te (2013)
    American Physical Society (APS)
    Details
    Publication Date: 2013-10-08
    Description: Author(s): E. E. Rodriguez, D. A. Sokolov, C. Stock, M. A. Green, O. Sobolev, Jose A. Rodriguez-Rivera, H. Cao, and A. Daoud-Aladine We construct a phase diagram of the parent compound Fe 1+ x Te as a function of interstitial iron x in terms of the electronic, structural, and magnetic properties. For a concentration of x 〈10%, Fe 1+ x Te undergoes a “semimetal” to metal transition at approximately 70 K that is also first-order and co... [Phys. Rev. B 88, 165110] Published Mon Oct 07, 2013
    Keywords: Electronic structure and strongly correlated systems
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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  • 4
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    Probing high-energy electronic excitations in NiO using inelastic neutron scattering (2011)
    American Physical Society (APS)
    Details
    Publication Date: 2011-08-30
    Description: Author(s): Young-June Kim, A. P. Sorini, C. Stock, T. G. Perring, J. van den Brink, and T. P. Devereaux High-energy local multiplet excitations of the d electrons are revealed in our inelastic neutron scattering measurements on the prototype magnetic insulator NiO. These become allowed by the presence of both nonzero crystal field and spin-orbit coupling. The observed excitations are consistent with o... [Phys. Rev. B 84, 085132] Published Mon Aug 29, 2011
    Keywords: Electronic structure and strongly correlated systems
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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  • 5
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    Magnetism of the Fe^{2+} and Ce^{3+} sublattices in Ce_{2}O_{2}FeSe_{2}: A combined neutron powder diffraction, inelastic neutron scattering, and density functional study (2014)
    American Physical Society (APS)
    Details
    Publication Date: 2014-12-10
    Description: Author(s): E. E. McCabe, C. Stock, J. L. Bettis, Jr., M.-H. Whangbo, and J. S. O. Evans The discovery of superconductivity in the 122 iron selenide materials above 30 K necessitates an understanding of the underlying magnetic interactions. We present a combined experimental and theoretical investigation of magnetic and semiconducting Ce 2 O 2 FeSe 2 composed of chains of edge-linked iron se... [Phys. Rev. B 90, 235115] Published Tue Dec 09, 2014
    Keywords: Electronic structure and strongly correlated systems
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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  • 6
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    Soft striped magnetic fluctuations competing with superconductivity in Fe1+xTe (2014)
    American Physical Society (APS)
    Details
    Publication Date: 2014-10-01
    Description: Author(s): C. Stock, E. E. Rodriguez, O. Sobolev, J. A. Rodriguez-Rivera, R. A. Ewings, J. W. Taylor, A. D. Christianson, and M. A. Green Neutron spectroscopy is used to investigate the magnetic fluctuations in Fe1+xTe—a parent compound of chalcogenide superconductors. Incommensurate “stripelike” excitations soften with increased interstitial iron concentration. The energy crossover from incommensurate to stripy fluctuations defines a... [Phys. Rev. B 90, 121113] Published Tue Sep 30, 2014
    Keywords: Electronic structure and strongly correlated systems
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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  • 7
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    Molecular architecture of the rotary motor in ATP synthase (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-11-27
    Description: Adenosine triphosphate (ATP) synthase contains a rotary motor involved in biological energy conversion. Its membrane-embedded F0 sector has a rotation generator fueled by the proton-motive force, which provides the energy required for the synthesis of ATP by the F1 domain. An electron density map obtained from crystals of a subcomplex of yeast mitochondrial ATP synthase shows a ring of 10 c subunits. Each c subunit forms an alpha-helical hairpin. The interhelical loops of six to seven of the c subunits are in close contact with the gamma and delta subunits of the central stalk. The extensive contact between the c ring and the stalk suggests that they may rotate as an ensemble during catalysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stock, D -- Leslie, A G -- Walker, J E -- New York, N.Y. -- Science. 1999 Nov 26;286(5445):1700-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10576729" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Catalysis ; Crystallization ; Crystallography, X-Ray ; Hydrogen Bonding ; Mitochondria/enzymology ; Models, Molecular ; Molecular Motor Proteins/*chemistry/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Proton-Motive Force ; Proton-Translocating ATPases/*chemistry/metabolism ; Protons ; Saccharomyces cerevisiae/enzymology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 8
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    The catalytic pathway of cytochrome p450cam at atomic resolution (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-03-04
    Description: Members of the cytochrome P450 superfamily catalyze the addition of molecular oxygen to nonactivated hydrocarbons at physiological temperature-a reaction that requires high temperature to proceed in the absence of a catalyst. Structures were obtained for three intermediates in the hydroxylation reaction of camphor by P450cam with trapping techniques and cryocrystallography. The structure of the ferrous dioxygen adduct of P450cam was determined with 0.91 angstrom wavelength x-rays; irradiation with 1.5 angstrom x-rays results in breakdown of the dioxygen molecule to an intermediate that would be consistent with an oxyferryl species. The structures show conformational changes in several important residues and reveal a network of bound water molecules that may provide the protons needed for the reaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schlichting, I -- Berendzen, J -- Chu, K -- Stock, A M -- Maves, S A -- Benson, D E -- Sweet, R M -- Ringe, D -- Petsko, G A -- Sligar, S G -- GM31756/GM/NIGMS NIH HHS/ -- GM33775/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Mar 3;287(5458):1615-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute for Molecular Physiology, Department of Physical Biochemistry, Otto Hahn Strasse 11, 44227 Dortmund, Germany. ilme.schlichting@mpi-dortmund.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10698731" target="_blank"〉PubMed〈/a〉
    Keywords: Camphor/*chemistry/*metabolism ; Camphor 5-Monooxygenase/*chemistry/*metabolism ; Catalysis ; Crystallization ; Crystallography, X-Ray ; Electrons ; Ferric Compounds/chemistry/metabolism ; Ferrous Compounds/chemistry/metabolism ; Hydrogen Bonding ; Hydroxylation ; Ligands ; Models, Molecular ; Molecular Conformation ; Oxygen/chemistry/metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protons ; Pseudomonas putida/enzymology ; Water/chemistry/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Structure of the torque ring of the flagellar motor and the molecular basis for rotational switching (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-08-03
    Description: The flagellar motor drives the rotation of flagellar filaments at hundreds of revolutions per second, efficiently propelling bacteria through viscous media. The motor uses the potential energy from an electrochemical gradient of cations across the cytoplasmic membrane to generate torque. A rapid switch from anticlockwise to clockwise rotation determines whether a bacterium runs smoothly forward or tumbles to change its trajectory. A protein called FliG forms a ring in the rotor of the flagellar motor that is involved in the generation of torque through an interaction with the cation-channel-forming stator subunit MotA. FliG has been suggested to adopt distinct conformations that induce switching but these structural changes and the molecular mechanism of switching are unknown. Here we report the molecular structure of the full-length FliG protein, identify conformational changes that are involved in rotational switching and uncover the structural basis for the formation of the FliG torque ring. This allows us to propose a model of the complete ring and switching mechanism in which conformational changes in FliG reverse the electrostatic charges involved in torque generation.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3159035/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3159035/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Lawrence K -- Ginsburg, Michael A -- Crovace, Claudia -- Donohoe, Mhairi -- Stock, Daniela -- MC_U105170645/Medical Research Council/United Kingdom -- P41 RR007707/RR/NCRR NIH HHS/ -- P41 RR007707-17/RR/NCRR NIH HHS/ -- RR007707/RR/NCRR NIH HHS/ -- Y1-CO-1020/CO/NCI NIH HHS/ -- Y1-GM-1104/GM/NIGMS NIH HHS/ -- Medical Research Council/United Kingdom -- England -- Nature. 2010 Aug 19;466(7309):996-1000. doi: 10.1038/nature09300. Epub 2010 Aug 1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Structural and Computational Biology Division, The Victor Chang Cardiac Research Institute, Lowy Packer Building, 405 Liverpool Street, Darlinghurst, New South Wales 2010, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20676082" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*chemistry/genetics/*metabolism ; Flagella/*chemistry/genetics/*physiology ; Models, Molecular ; Molecular Motor Proteins/*chemistry/genetics/metabolism ; Molecular Sequence Data ; Mutation ; Protein Conformation ; Protein Multimerization ; Protein Structure, Tertiary ; *Rotation ; Static Electricity ; Structure-Activity Relationship ; Thermotoga maritima/chemistry ; *Torque
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 10
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    Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-28
    Description: The three-dimensional structure of the proteasome from the archaebacterium Thermoplasma acidophilum has been elucidated by x-ray crystallographic analysis by means of isomorphous replacement and cyclic averaging. The atomic model was built and refined to a crystallographic R factor of 22.1 percent. The 673-kilodalton protease complex consists of 14 copies of two different subunits, alpha and beta, forming a barrel-shaped structure of four stacked rings. The two inner rings consist of seven beta subunits each, and the two outer rings consist of seven alpha subunits each. A narrow channel controls access to the three inner compartments. The alpha 7 beta 7 beta 7 alpha 7 subunit assembly has 72-point group symmetry. The structures of the alpha and beta subunits are similar, consisting of a core of two antiparallel beta sheets that is flanked by alpha helices on both sides. The binding of a peptide aldehyde inhibitor marks the active site in the central cavity at the amino termini of the beta subunits and suggests a novel proteolytic mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lowe, J -- Stock, D -- Jap, B -- Zwickl, P -- Baumeister, W -- Huber, R -- New York, N.Y. -- Science. 1995 Apr 28;268(5210):533-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Biochemie, Abteilung fur Strukturforschung, Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7725097" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Archaeal Proteins ; Binding Sites ; Chaperonin 60/chemistry ; Computer Graphics ; Crystallography, X-Ray ; Cysteine Endopeptidases/*chemistry/metabolism ; Endopeptidases/*chemistry/metabolism ; Fourier Analysis ; Hydrogen Bonding ; Leupeptins/chemistry/metabolism ; *Models, Molecular ; Molecular Sequence Data ; Multienzyme Complexes/*chemistry/metabolism ; Protease Inhibitors/chemistry/metabolism ; Proteasome Endopeptidase Complex ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Proteins/metabolism ; Thermoplasma/*enzymology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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