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  • Journal article
    Beeby M, Bobik TA, Yeates TO, 2009,

    Exploiting genomic patterns to discover new supramolecular protein assemblies

    , Protein Sci., Vol: 18, Pages: 69-79
  • Journal article
    Iguchi A, Thomson NR, Ogura Y, Saunders D, Ooka T, Henderson IR, Harris D, Asadulghani M, Kurokawa K, Dean P, Kenny B, Quail MA, Thurston S, Dougan G, Hayashi T, Parkhill J, Frankel Get al., 2009,

    , JOURNAL OF BACTERIOLOGY, Vol: 191, Pages: 347-354, ISSN: 0021-9193
    • Cite
    • Citations: 275
  • Journal article
    Hare S, Shun M-C, Gupta SS, Valkov E, Engelman A, Cherepanov Pet al., 2009,

    , PLOS PATHOGENS, Vol: 5, ISSN: 1553-7366
    • Cite
    • Citations: 127
  • Journal article
    McGeehan J, Ravelli RBG, Murray JW, Owen RL, Cipriani F, McSweeney S, Weik M, Garman EFet al., 2009,

    Colouring cryo-cooled crystals: online microspectrophotometry

    , Journal of Synchrotron Radiation, Vol: 16, Pages: 163-172

    X-rays can produce a high concentration of radicals within cryo-cooled macromolecular crystals. Some radicals have large extinction coefficients in the visible (VIS) range of the electromagnetic spectrum, and can be observed optically and spectrally. An online microspectrophotometer with high temporal resolution has been constructed that is capable of measuring UV/VIS absorption spectra (200-1100 nm) during X-ray data collection. The typical X-ray-induced blue colour that is characteristic of a wide range of cryo-conditions has been identified as trapped solvated electrons. Disulphide-containing proteins are shown to form disulphide radicals at millimolar concentrations, with absorption maxima around 400 nm. The solvated electrons and the disulphide radicals seem to have a lifetime in the range of seconds up to minutes at 100 K. The temperature dependence of the kinetics of X-ray-induced radical formation is different for the solvated electrons compared with the disulphide radicals. The online microspectrophotometer provides a technique complementary to X-ray diffraction for analysing and characterizing intermediates and redox states of proteins and enzymes.
  • Journal article
    Hare S, Cherepanov P, 2009,

    , Viruses, Vol: 1, Pages: 780-801
  • Journal article
    Mackiewicz N, Delaire JA, Rutherford AW, Doris E, Mioskowski Cet al., 2009,

    , CHEMISTRY-A EUROPEAN JOURNAL, Vol: 15, Pages: 3882-3888, ISSN: 0947-6539
    • Cite
    • Citations: 12
  • Journal article
    Robinson T, Schaerli Y, Wootton R, Hollfelder F, Dunsby C, Baldwin G, Neil M, French P, deMello Aet al., 2009,

    , LAB ON A CHIP, Vol: 9, Pages: 3437-3441, ISSN: 1473-0197
    • Cite
    • Citations: 30
  • Journal article
    van Thor JJ, 2009,

    Photoreactions and dynamics of the green fluorescent protein

    , Chem Soc Rev, Vol: 38, Pages: 2935-2950

    The wild type green fluorescent protein (GFP) from Aequorea victoria has been extensively investigated with a strong focus on the photochemistry and structural dynamics that are linked with its diverse activities. GFP combines a number of remarkable, and some unique, features that are still intensely researched both experimentally and theoretically. The protein environment effectively inhibits deactivation pathways that are dominant in the isolated chromophore and is therefore responsible for the bright fluorescence. Its p-hydroxybenzylidene-imidazolidinone chromophore acts as a photoacid, and optical excitation triggers ultrafast proton transfer reactions in the active site. The microscopic details of the proton transfer mechanism through a hydrogen bonding network are discussed in this critical review. This property of the wild type GFP has provided the opportunity to characterise the role of the specific protein environment in the proton transfer reactions in comparison to photoacid reactions in the condensed phase. In addition, GFP displays a photochromic side reaction that is uniquely caused by electron transfer from a buried anionic glutamic acid to the optically excited chromophore. This phototransformation property has also been exploited in high resolution fluorescence microscopy techniques. The discussion in this review is extended to include vibrational spectroscopy and structural dynamics (106 references).
  • Journal article
    Komatsu T, Nakagawa A, Curry S, Tsuchida E, Murata K, Nakamura N, Ohno Het al., 2009,

    , ORGANIC & BIOMOLECULAR CHEMISTRY, Vol: 7, Pages: 3836-3841, ISSN: 1477-0520
    • Cite
    • Citations: 13
  • Journal article
    Wilderen LJGWV, Clark IP, Towrie M, Thor JJV, van Thor JJet al., 2009,

    Mid-infrared picosecond pump-dump-probe and pump-repump-probe experiments to resolve a ground-state intermediate in cyanobacterial phytochrome Cph1

    , J Phys Chem B, Vol: 113, Pages: 16354-16364

    Multipulse picosecond mid-infrared spectroscopy has been used to study photochemical reactions of the cyanobacterial phytochrome photoreceptor Cph1. Different photophysical schemes have been discussed in the literature to describe the pathways after photoexcitation, particularly, to identify reaction phases that are linked to photoisomerisation and electronic decay in the 1566-1772 cm(-1) region that probes C=C and C=O stretching modes of the tetrapyrrole chromophore. Here, multipulse spectroscopy is employed, where, compared to conventional visible pump-mid-infrared probe spectroscopy, an additional visible pulse is incorporated that interacts with populations that are evolving on the excited- and ground-state potential energy surfaces. The time delays between the pump and the dump pulse are chosen such that the dump pulse interacts with different phases in the reaction process. The pump and dump pulses are at the same wavelength, 640 nm, and are resonant with the Pr ground state as well as with the excited state and intermediates. Because the dump pulse additionally pumps the remaining, partially recovered, and partially oriented ground-state population, theory is developed for estimating the fraction of excited-state molecules. The calculations take into account the model-dependent ground-state recovery fraction, the angular dependence of the population transfer resulting from the finite bleach that occurs with linearly polarized intense femtosecond optical excitation, and the partially oriented population for the dump field. Distinct differences between the results from the experiments that use a 1 or a 14 ps dump time favor a branching evolution from S1 to an excited state or reconfigured chromophore and to a newly identified ground-state intermediate (GSI). Optical dumping at 1 ps shows the instantaneous induced absorption of a delocalized C=C stretching mode at 1608 cm(-1), where the increased cross section is associated with the electronic ground-state struc
  • Journal article
    Lou H, Beis K, Naismith JH, 2009,

    , MEMBRANE PROTEIN CRYSTALLIZATION, Vol: 63, Pages: 269-297, ISSN: 1063-5823
  • Journal article
    Curry S, 2009,

    , DRUG METABOLISM AND PHARMACOKINETICS, Vol: 24, Pages: 342-357, ISSN: 1347-4367
    • Cite
    • Citations: 258
  • Journal article
    Luther PK, Bennett PM, Knupp C, Craig R, Padron R, Harris SP, Patel J, Moss RLet al., 2008,

    , JOURNAL OF MOLECULAR BIOLOGY, Vol: 384, Pages: 60-72, ISSN: 0022-2836
    • Cite
    • Citations: 105
  • Journal article
    Hohenester E, Sasaki T, Giudici C, Farndale RW, Baechinger HPet al., 2008,

    , PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 105, Pages: 18273-18277, ISSN: 0027-8424
    • Cite
    • Citations: 113
  • Journal article
    Bose D, Pape T, Burrows PC, Rappas M, Wigneshweraraj SR, Buck M, Zhang Xet al., 2008,

    , MOLECULAR CELL, Vol: 32, Pages: 337-346, ISSN: 1097-2765
    • Cite
    • Citations: 61
  • Journal article
    Schenderlein M, Cetin M, Barber J, Telfer A, Schlodder Eet al., 2008,

    , BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, Vol: 1777, Pages: 1400-1408, ISSN: 0005-2728
    • Cite
    • Citations: 25
  • Journal article
    Marles-Wright J, Grant T, Delumeau O, van Duinen G, Firbank SJ, Lewis PJ, Murray JW, Newman JA, Quin MB, Race PR, Rohou A, Tichelaar W, van Heel M, Lewis RJet al., 2008,

    , SCIENCE, Vol: 322, Pages: 92-96, ISSN: 0036-8075
    • Cite
    • Citations: 132
  • Journal article
    Cser K, Deak Z, Telfer A, Barber J, Vass Iet al., 2008,

    , PHOTOSYNTHESIS RESEARCH, Vol: 98, Pages: 131-140, ISSN: 0166-8595
    • Cite
    • Citations: 20
  • Journal article
    Carpenter EP, Beis K, Cameron AD, Iwata Set al., 2008,

    , CURRENT OPINION IN STRUCTURAL BIOLOGY, Vol: 18, Pages: 581-586, ISSN: 0959-440X
    • Cite
    • Citations: 372
  • Journal article
    Murray JW, Maghlaoui K, Kargul J, Sugiura M, Barber Jet al., 2008,

    , PHOTOSYNTHESIS RESEARCH, Vol: 98, Pages: 523-527, ISSN: 0166-8595
    • Cite
    • Citations: 24
  • Journal article
    Bailleul B, Johnson X, Finazzi G, Barber J, Rappaport F, Telfer Aet al., 2008,

    , JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 283, Pages: 25218-25226
    • Cite
    • Citations: 22
  • Journal article
    Yla-Maihaniemi PP, Heng JYY, Thielmann F, Williams DRet al., 2008,

    , LANGMUIR, Vol: 24, Pages: 9551-9557, ISSN: 0743-7463
    • Cite
    • Citations: 95
  • Journal article
    Lossi NS, Rolhion N, Magee AI, Boyle C, Holden DWet al., 2008,

    , MICROBIOLOGY-SGM, Vol: 154, Pages: 2680-2688, ISSN: 1350-0872
    • Cite
    • Citations: 68
  • Journal article
    Zunszain PA, Ghuman J, McDonagh AF, Curry Set al., 2008,

    , JOURNAL OF MOLECULAR BIOLOGY, Vol: 381, Pages: 394-406, ISSN: 0022-2836
    • Cite
    • Citations: 244
  • Journal article
    Robinson T, Valluri P, Manning HB, Owen DM, Munro I, Talbot CB, Dunsby C, Eccleston JF, Baldwin GS, Neil MAA, de Mello AJ, French PMWet al., 2008,

    , OPTICS LETTERS, Vol: 33, Pages: 1887-1889, ISSN: 0146-9592
    • Cite
    • Citations: 19
  • Journal article
    Bodvarsson B, Klim S, Morkebjerg M, Mortensen S, Yoon CH, Chen J, Maclaren JR, Luther PK, Squire JM, Bones PJ, Millane RPet al., 2008,

    , IMAGE AND VISION COMPUTING, Vol: 26, Pages: 1073-1080, ISSN: 0262-8856
  • Journal article
    Burrows PC, Wigneshweraraj S, Bose D, Joly N, Schumacher J, Rappas M, Pape T, Stockley PG, Zhang X, Buck Met al., 2008,

    , BIOCHEMICAL SOCIETY TRANSACTIONS, Vol: 36, Pages: 776-779, ISSN: 0300-5127
  • Journal article
    Fukuhara N, Howitt JA, Hussain S-A, Hohenester Eet al., 2008,

    , JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 283, Pages: 16226-16234, ISSN: 0021-9258
    • Cite
    • Citations: 68
  • Journal article
    Filloux A, Hachani A, Bleves S, 2008,

    , Microbiology, Vol: 154, Pages: 1570-1583, ISSN: 1350-0872
  • Journal article
    Pommet M, Juntaro J, Heng JYY, Mantalaris A, Lee AF, Wilson K, Kalinka G, Shaffer MSP, Bismarck Aet al., 2008,

    , BIOMACROMOLECULES, Vol: 9, Pages: 1643-1651, ISSN: 1525-7797
    • Cite
    • Citations: 206

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