The research involved 19 institutions from eight countries and four continents. These institution... more The research involved 19 institutions from eight countries and four continents. These institutional partners engaged in fact-finding and theory generation with the common aim of informing current and future employability policies and practices. This work aligned with the diverse aspirations of all higher education stakeholders and fostered communication between colleagues through open dialogue. The core research question was: How is employability termed, driven, and communicated by universities internationally?
Journal of Teaching and Learning for Graduate Employability
Career development learning has a demonstrable positive impact on the graduate employability of h... more Career development learning has a demonstrable positive impact on the graduate employability of higher education learners. This is particularly the case if it is integrated into the curriculum rather than experienced as an add-on or included in finite curriculum elements. However, integration of career development learning into curriculum is a significant and challenging undertaking in course design, and also in facilitation of learning experiences. Academics manage crowded curricula in their disciplinary areas, and many also have external course accreditation requirements to deal with that may not include career development elements. In many institutions there is mixed understanding of what career development learning entails, no clear top-level strategic support, and unprecedented numbers of enrolled students across digital and on-campus provision. This article explores challenges and opportunities in integrating career development learning into curriculum in higher education, and...
Review of DVD—‘Reflective Career Counselling’ Enabling Reflection in Career Counselling Based on Career Construction Principles and Practises by Jacobus G. Maree, University of Pretoria, South Africa
Acta Crystallographica Section C Crystal Structure Communications, 1992
8-Methoxy-2-(n-propylamino)tetralin (8MeO-PAT) hydrochloride, CI4H22NO + .CI-, Mr = 255.8, monocl... more 8-Methoxy-2-(n-propylamino)tetralin (8MeO-PAT) hydrochloride, CI4H22NO + .CI-, Mr = 255.8, monoclinic, F21/n, a=9.2229(4), * Lists of structure factors, anisotropic thermal parameters and H-atom parameters have been deposited with the British Library Document Supply Centre as Supplementary Publication No. SUP 54590 (27 pp.). Copies may be obtained through The Technical Editor, International Union of Crystallography, 5 Abbey Square, Chester CHI 2HU, England.
Acta crystallographica. Section C, Crystal structure communications, Jan 15, 1990
7-(3-[1-(4-Phenylthiosemicarbazono)ethyl]-bicyclo[2.2.1]hept-2- yl)-5-heptenoic acid, C23H31N3-O2... more 7-(3-[1-(4-Phenylthiosemicarbazono)ethyl]-bicyclo[2.2.1]hept-2- yl)-5-heptenoic acid, C23H31N3-O2S, Mr = 413.7, monoclinic, P2(1)/a, a = 12.9650 (7), b = 11.2081 (6), c = 16.8941 (12) A, beta = 110.452 (5) degrees, V = 2300.2 A3, Z = 4, Dx = 1.194 g cm-3, Mo K alpha, lambda = 0.71073 A, mu = 1.55 cm-1, F(000) = 888, T = 298 K. Final R = 0.0472 with 2778 independent data. EP 092 is a thromboxane receptor antagonist akin to many other analogues of the thromboxane A2 [Wilson & Jones (1985). Adv. Prostaglandin Thromboxane Leukotriene Res. 14, 393-425].
DMSO reductase (DMSOR) from Rhodobacter capsulatus, well-characterised as a molybdoenzyme, will b... more DMSO reductase (DMSOR) from Rhodobacter capsulatus, well-characterised as a molybdoenzyme, will bind tungsten. Protein crystallography has shown that tungsten in W-DMSOR is ligated by the dithiolene group of the two pyranopterins, the oxygen atom of Ser147 plus another oxygen atom, and is located in a very similar site to that of molybdenum in Mo-DMSOR. These conclusions are consistent with W L III-edge X-ray absorption, EPR and UV/visible spectroscopic data. W-DMSOR is signi®cantly more active than Mo-DMSOR in catalysing the reduction of DMSO but, in contrast to the latter, shows no signi®cant ability to catalyse the oxidation of DMS.
The crystal structure of the molybdenum enzyme dimethylsulphoxide reductase (DMSOR) has been dete... more The crystal structure of the molybdenum enzyme dimethylsulphoxide reductase (DMSOR) has been determined at 1.9 A Ê resolution with substrate bound at the active site. DMSOR is an oxotransferase which catalyses the reduction of dimethylsulphoxide (DMSO) to dimethylsulphide (DMS) in a two stage reaction which is linked to oxygen atom transfer and electron transfer. In the ®rst step, DMSO binds to reduced (Mo (IV)) enzyme, the enzyme is oxidised to Mo (VI) with an extra oxygen ligand and DMS is released. Regeneration of reduced enzyme is achieved by transfer of two electrons, successively from a speci®c cytochrome, and release of the oxygen as water. The enzyme, puri®ed under aerobic conditions, is in the oxidised (Mo (VI)) state. Addition of a large excess of DMS to the oxidised enzyme in solution causes a change in the absorption spectrum of the enzyme. The same reaction occurs within crystals of the enzyme and the crystal structure reveals a complex with DMSO bound to the molybdenum via its oxygen atom. X-ray edge data indicate that the metal is in the Mo (IV) state. The DMSO ligand replaces one of the two oxo groups which ligate the oxidised form of the enzyme, suggesting very strongly that this is the oxygen which is transferred during catalysis. Residues 384 to 390, disordered in the oxidised enzyme, are now clearly seen in the cleft leading to the active site. The side-chain of Trp388 forms a lid trapping the substrate/product.
The "prismane" protein resolved: X-ray structure at 1.7 Å and multiple spectroscopy of two novel 4Fe clusters
Journal of Biological Inorganic Chemistry, 1998
AF Arendsen 7 J. Hadden 7 G. Card 7 AS McAlpine S. Bailey 7 V. Zaitsev 7 EHM Duke 7 PF Lindley1 C... more AF Arendsen 7 J. Hadden 7 G. Card 7 AS McAlpine S. Bailey 7 V. Zaitsev 7 EHM Duke 7 PF Lindley1 CCLRC Daresbury Laboratory, Warrington WA4 4AD, UK M. Kröckel 7 AX Trautwein Institut für Physik, Medizinische Universität, D-23538 Lübeck, Germany MC Feiters ...
X-ray absorption spectroscopy of dimethylsulfoxide reductase from Rhodobacter capsulatus
Journal of Biological Inorganic Chemistry, 1997
... Philippa E. Baugh 7 C. David Garner John M. Charnock 7 David Collison E. Stephen Davies 7 Ala... more ... Philippa E. Baugh 7 C. David Garner John M. Charnock 7 David Collison E. Stephen Davies 7 Alan S. McAlpine 7 Sue Bailey Ian ... shells of back-scattering atoms around the central absorber atom and iter-ating the absorber-scatterer distances, r, the Debye-Waller type factors ...
Calorimetric measurements of binding of a specific DNA fragment and S-adenosyl methionine (SAM) c... more Calorimetric measurements of binding of a specific DNA fragment and S-adenosyl methionine (SAM) co-repressor molecules to the E. coli methionine repressor (MetJ) show significant differences in the energetics of binary and ternary protein-DNA complexes. Formation of the MetJ: SAM : DNA ternary complex is significantly more exothetmic (LIH =-99 kJ. mol-') than either MetJ: DNA or MetJ: SAM binary complexes alone (AH =-10 kJ.mol-' each). The protein is also significantly more stable to unfolding (AT, = 5.4"C) when bound to DNA. These observations suggest that binding of SAM to the protein-DNA complex leads to a significant reduction in dynamic flexibility of the ternary complex, with considerable entropyenthalpy compensation, not necessarily involving any overall conformational change.
Background: Mammalian purple acid phosphatases are highly conserved binuclear metal-containing en... more Background: Mammalian purple acid phosphatases are highly conserved binuclear metal-containing enzymes produced by osteoclasts, the cells that resorb bone. The enzyme is a target for drug design because there is strong evidence that it is involved in bone resorption. Results: The 1.55 Å resolution structure of pig purple acid phosphatase has been solved by multiple isomorphous replacement. The enzyme comprises two sandwiched β sheets flanked by α-helical segments. The molecule shows internal symmetry, with the metal ions bound at the interface between the two halves. Conclusions: Despite less than 15% sequence identity, the protein fold resembles that of the catalytic domain of plant purple acid phosphatase and some serine/threonine protein phosphatases. The active-site regions of the mammalian and plant purple acid phosphatases differ significantly, however. The internal symmetry suggests that the binuclear centre evolved as a result of the combination of mononuclear ancestors. The structure of the mammalian enzyme provides a basis for antiosteoporotic drug design.
Acta Crystallographica Section D Biological Crystallography, 1996
Dimethylsulfoxide reductase from the photosynthetic bacterium Rhodobacter capsulatus has been cry... more Dimethylsulfoxide reductase from the photosynthetic bacterium Rhodobacter capsulatus has been crystallized in two similar forms which are suitable for X-ray structure determination. Both crystals forms belong to space group P4~22 or P4322, with cell dimensions a=b=80.81, c = 229.75 A, (type I crystals) or a = b = 89.30, c = 230.05 A, (type II crystals) and one molecule in the asymmetric unit. Diffraction has been observed to at least 2.0 A, in type I crystals and to 2.6 A, in type II crystals. Dimethylsulfoxide reductase from Rhodobacter is the simplest molybdenum oxotransferase known and this makes it an ideal model to study the structure and function of this class of enzymes.
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