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Structural polymorphism in a tubercidin analogue of the DNA double helix

Autor: Darren J Hughes, Trevor Forsyth, Watson Fuller, M.W. Shotton, L. H. Pope, R. C. Denny

Publikováno v: ResearcherID

A high-angle X-ray fibre diffraction study of a tubercidin analogue of the poly[d(A-T)]·poly[d(A-T)] DNA double helix has been carried out using station 7.2 at the Daresbury Laboratory synchrotron radiation source. The polymer has been studied for a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e199a244d722fac2b4893d5d3e83b042
https://doi.org/10.1016/s0301-4622(97)00132-4

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Myosin Rod-Packing Schemes in Vertebrate Muscle Thick Filaments

Autor: John M. Squire, Pradeep K. Luther, Marie E. Cantino, Michael Chew, R. C. Denny, Liam Hudson, Jeff Harford

Publikováno v: Journal of Structural Biology. 122:128-138

Muscle myosin filament backbones are known to be aggregates of long coiled-coil alpha-helical myosin rods, but the packing arrangement is not understood in detail. Here we present new data on fish muscle myosin filaments from low-angle X-ray diffract

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f3dccb83678fd290e1767ef883de481
https://doi.org/10.1006/jsbi.1998.3995

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A high-angle neutron fibre diffraction study of the hydration of deuterated A-DNA

Autor: U. Giesen, Paul Langan, Marie-Therese Dauvergne, R. C. Denny, L. H. Pope, Trevor Forsyth, Watson Fuller, M.W. Shotton

Publikováno v: ResearcherID

A high-angle neutron fibre diffraction study of the hydration of A-DNA has been performed using the single-crystal diffractometer D19 at the Institut Laue-Langevin (Grenoble, France). The sample was prepared using deuterated DNA extracted from E. Col

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83052dc7c2060ae4592e12247fa92e31
https://doi.org/10.1016/s0301-4622(97)00090-2

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Myosin head configuration in relaxed fish muscle: resting state myosin heads must swing axially by up to 150 Å or turn upside down to reach rigor

Autor: Jeffrey J. Harford, Liam Hudson, R. C. Denny, John M. Squire

Publikováno v: Journal of Molecular Biology. 273:440-455

The arrangement and shape of myosin heads in relaxed muscle have been determined by analysis of low-angle X-ray diffraction data from a very highly ordered vertebrate muscle in bony fish. This reveals the arrangement and interactions between the two

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f5fba0257ef8151f557dc440a6da260
https://doi.org/10.1006/jmbi.1997.1321

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Collecting and Processing Neutron Fibre Diffraction Data from a Single-Crystal Diffractometer

Autor: Paul Langan, Arumugam Mahendrasingam, A. Jaber, Sax A. Mason, R. C. Denny

Publikováno v: Journal of Applied Crystallography. 29:383-389

The geometries for scanning reciprocal space for a fibre on a neutron single-crystal diffractometer are considered. Geometrical relationships are derived for the particular case of D19 at the Institut Laue-Langevin that can be readily generalized for

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::175fff85c6b9c08763e5ceae1e7a4511
https://doi.org/10.1107/s0021889896002816

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Myosin Crossbridge Configurations in Equilibrium States of Vertebrate Skeletal Muscle

Autor: Liam Hudson, John M. Squire, Michael Chew, Marie Cantino, Pradeep K. Luther, R. C. Denny, Jeff Harford, Robert A. Mendelson, Edward P. Morris

Publikováno v: Advances in Experimental Medicine and Biology ISBN: 9781468460414

The positions and orientations of the myosin heads in relaxed, active, rigor and S1-labelled fish muscle are being determined by analysis both of electron micrographs and of low-angle X-ray diffraction patterns. The X-ray analysis of resting muscle m

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9d5a2ab7a86927993a6bb1d67600a644
https://doi.org/10.1007/978-1-4684-6039-1_35

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Structure determination of OppA at 2.3 A resolution using multiple-wavelength anomalous dispersion methods

Autor: Anthony J. Wilkinson, R. C. Denny, Andrew Thompson, I. D. Glover, N. D. Nguti, S. H. Kinder, Jeremy R. H. Tame, Sean McSweeney, Eleanor J. Dodson

Publikováno v: Acta crystallographica. Section D, Biological crystallography. 51(Pt 1)

OppA is a 58.8 kDa bacterial transport protein involved in the transport of peptides across the cytoplasmic membrane of Gram-negative bacteria. It binds peptides from two to five residues in length but with little sequence specificity. OppA from Salm

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0be344c1326933283b38783f59a265f3
https://pubmed.ncbi.nlm.nih.gov/15299334

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