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  • 1
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    Coupled short-range ferroelectric and magnetic order in PbFe_{1/2}Nb_{1/2}O_{3} (2013)
    American Physical Society (APS)
    Details
    Publication Date: 2013-09-14
    Description: Author(s): C. Stock, S. R. Dunsiger, R. A. Mole, X. Li, and H. Luo A neutron scattering investigation of the magnetoelectric coupling in PbFe 1/2 Nb 1/2 O 3 has been undertaken. Ferroelectric order occurs below 400 K, as evidenced by the softening with temperature and subsequent recovery of the zone center transverse optic phonon mode energy ( ℏ Ω 0 ). Over the same tempera... [Phys. Rev. B 88, 094105] Published Fri Sep 13, 2013
    Keywords: Structure, structural phase transitions, mechanical properties, defects
    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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    Freezing of the local dynamics in the relaxor ferroelectric [Pb(Zn_{1/3}Nb_{2/3})O_{3}]_{0.955}[PbTiO_{3}]_{0.045} (2012)
    American Physical Society (APS)
    Details
    Publication Date: 2012-10-06
    Description: Author(s): Zhijun Xu, Jinsheng Wen, E. Mamontov, C. Stock, P. M. Gehring, and Guangyong Xu We report measurements of the neutron diffuse scattering in a single crystal of the relaxor ferroelectric material 95.5%Pb(Zn 1/3 Nb 2/3 )O 3 -4.5%PbTiO 3 (PZN-4.5%PT). We show that the diffuse scattering at high temperatures has a quasielastic component with energy width ≳0.1 meV. On cooling the total dif... [Phys. Rev. B 86, 144106] Published Fri Oct 05, 2012
    Keywords: Structure, structural phase transitions, mechanical properties, defects
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
    Published by American Physical Society (APS)
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  • 3
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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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  • 4
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    Predicting coiled coils from protein sequences (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-05-24
    Description: The probability that a residue in a protein is part of a coiled-coil structure was assessed by comparison of its flanking sequences with sequences of known coiled-coil proteins. This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions of discontinuity within coiled-coil structures, such as the hinge region in myosin. More than 200 proteins that probably have coiled-coil domains were identified in GenBank, including alpha- and beta-tubulins, flagellins, G protein beta subunits, some bacterial transfer RNA synthetases, and members of the heat shock protein (Hsp70) family.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lupas, A -- Van Dyke, M -- Stock, J -- AI20980/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1991 May 24;252(5009):1162-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, NJ 08544.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2031185" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/chemistry ; Animals ; Databases, Factual ; Humans ; Probability ; *Protein Conformation ; Proteins/chemistry/*genetics
    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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  • 5
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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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  • 6
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    Proteasome from Thermoplasma acidophilum: a threonine protease (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-28
    Description: The catalytic mechanism of the 20S proteasome from the archaebacterium Thermoplasma acidophilum has been analyzed by site-directed mutagenesis of the beta subunit and by inhibitor studies. Deletion of the amino-terminal threonine or its mutation to alanine led to inactivation of the enzyme. Mutation of the residue to serine led to a fully active enzyme, which was over ten times more sensitive to the serine protease inhibitor 3,4-dichloroisocoumarin. In combination with the crystal structure of a proteasome-inhibitor complex, the data show that the nucleophilic attack is mediated by the amino-terminal threonine of processed beta subunits. The conservation pattern of this residue in eukaryotic sequences suggests that at least three of the seven eukaryotic beta-type subunit branches should be proteolytically inactive.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seemuller, E -- Lupas, A -- Stock, D -- Lowe, J -- Huber, R -- Baumeister, W -- New York, N.Y. -- Science. 1995 Apr 28;268(5210):579-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Abteilung fur Strukturbiologie Max-Planck Institut fur Biochemie, Martinsried, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7725107" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Archaeal Proteins ; Binding Sites ; Coumarins/pharmacology ; Endopeptidases/*chemistry/metabolism ; Hydrogen-Ion Concentration ; Molecular Sequence Data ; Mutagenesis ; Protein Folding ; Sequence Alignment ; Serine Proteinase Inhibitors/pharmacology ; Thermoplasma/*enzymology
    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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  • 7
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    Evidence for anisotropic polar nanoregions in relaxor Pb(Mg_{1/3}Nb_{2/3})O_{3}: A neutron study of the elastic constants and anomalous TA phonon damping in PMN (2012)
    American Physical Society (APS)
    Details
    Publication Date: 2012-09-19
    Description: Author(s): C. Stock, P. M. Gehring, H. Hiraka, I. Swainson, Guangyong Xu, Z.-G. Ye, H. Luo, J.-F. Li, and D. Viehland We use neutron inelastic scattering to characterize the acoustic phonons in the relaxor Pb(Mg 1/3 Nb 2/3 )O 3 (PMN) and demonstrate the presence of a highly anisotropic damping mechanism that is directly related to short-range polar correlations. For a large range of temperatures above T c ∼210  K, where d... [Phys. Rev. B 86, 104108] Published Tue Sep 18, 2012
    Keywords: Structure, structural phase transitions, mechanical properties, defects
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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  • 8
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    Molecular orientational melting within a lead-halide octahedron framework: The order-disorder transition in ${\mathrm{CH}}_{3}{\mathrm{NH}}_{3}{\mathrm{PbBr}}_{3}$ (2017)
    American Physical Society (APS)
    Details
    Publication Date: 2017-11-23
    Description: Author(s): K. L. Brown, S. F. Parker, I. Robles García, S. Mukhopadhyay, V. García Sakai, and C. Stock Lead-halide organic-inorganic perovskites consist of an inorganic host framework with an organic molecule occupying the interstitial space. The structure and dynamics of these materials have been heavily studied recently due to interest in their exceptional photovoltaic properties. We combine inelas... [Phys. Rev. B 96, 174111] Published Wed Nov 22, 2017
    Keywords: Structure, structural phase transitions, mechanical properties, defects
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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  • 9
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    Inelastic x-ray investigation of the ferroelectric transition in SnTe (2017)
    American Physical Society (APS)
    Details
    Publication Date: 2017-04-04
    Description: Author(s): Christopher D. O'Neill, Dmitry A. Sokolov, Andreas Hermann, Alexei Bossak, Christopher Stock, and Andrew D. Huxley We report that the lowest energy transverse-optic phonon in metallic SnTe softens to near zero energy at the structural transition at T C = 75 K and importantly show that the energy of this mode below T C increases as the temperature decreases. Since the mode is a polar displacement this proves unambiguo… [Phys. Rev. B 95, 144101] Published Mon Apr 03, 2017
    Keywords: Structure, structural phase transitions, mechanical properties, defects
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
    Published by American Physical Society (APS)
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