967 resultados para Bioethics and Medical Ethics


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Samuel Taylor Coleridge.--Frederick Denison Maurice.--Thomas Erskine of Linlathen.--Life of Charles Kingsley.--Arthur Penrhyn Stanley.--The Cambridge apostles of 1830.--Richard Holt Hutton.--A study of Carlyle.--The majority.--James Fitzjames Stephen.--The moral influence of George Eliot.--John Ruskin.--Laurence Oliphant.--Count Leo Tolstoi.--Morals and politics.--Ethics and science.--Biography.--The relation of memory to will.--The vanity of men of letters.--Invalids.--Apologies.--Henry Thomas Buckle.--The unfaithful steward.--Brothers, an address to female students.--De senectute.--The drawbacks of the intellectual life.

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Includes bibliographical references and index.

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Examines health and medical facilities in Africa south of Sahara and considers needs and opportunities for U.S. private investment in Africa.

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Thesis (Master's)--University of Washington, 2016-06

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Thesis (Master's)--University of Washington, 2016-06

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Thesis (Ph.D.)--University of Washington, 2016-06

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Thesis (Ph.D.)--University of Washington, 2016-06

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Thesis (Master's)--University of Washington, 2016-06

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Objective: To survey the attitudes of Australian medical students to determine their views about the relative attractiveness of psychiatry as a career compared with other specialities, and against findings from a North American study. Method: We surveyed 655 first-year medical students attending six Australian Universities. Results: Responses indicated that Australian medical students view psychiatry as distinctly less 'attractive' than other career options, as reported in the North American sample. In comparison with other disciplines, psychiatry was regarded as more interesting and intellectually challenging, but also as lacking a scientific foundation, not being enjoyable and failing to draw on training experiences. Conclusion: Our findings suggest that psychiatry has an image problem that is widespread, reflecting Community perceptions and the specialist interests of medical students on recruitment. If psychiatry is to improve its 'attractiveness' as a career option, identified image problems need to be corrected and medical student selection processes re-considered.

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Biological utilisation of copper requires that the metal, in its ionic forms, be meticulously transported, inserted into enzymes and regulatory proteins, and excess be excreted. To understand the trafficking process, it is crucial that the structures of the proteins involved in the varied processes be resolved. To investigate copper binding to a family of structurally related copper-binding proteins, we have characterised the second Menkes N-terminal domain (MNKr2). The structure, determined using H-1 and N-15 heteronuclear NMR, of the reduced form of MNKr2 has revealed two alpha-helices lying over a single beta-sheet and shows that the binding site, a Cys(X)(2)Cys pair, is located on an exposed loop. H-1-N-15 HSQC experiments demonstrate that binding of Cu(I) causes changes that are localised to conserved residues adjacent to the metal binding site. Residues in this area are important to the delivery of copper by the structurally related Cu(I) chaperones. Complementary site-directed mutagenesis of the adjacent residues has been used to probe the structural roles of conserved residues. (C) 2003 Published by Elsevier Inc.

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Rationale and Objectives. The authors attempt to provide a set of objectives for medical student training in radiology for contemporary medical practice. Materials and Methods. A questionnaire containing a list of educational objectives was sent to 32 radiologists in charge of medical student training in radiology at accredited residency programs in Australia and New Zealand. The importance of including each preselected objective in the curriculum was measured by respondents' agreement or disagreement on a scale of 1-6. Opportunity also was given to respondents to suggest objectives other than those presented on the questionnaire. Results. Twenty of the 32 questionnaires were returned, and a set of educational objectives was established based on the responses. The objectives were ranked in importance according to the mean score assigned to each objective by the respondents. Conclusion. This new set of educational objectives for medical student radiology training reflects recent changes in radiologic and medical practice and points to potential future developments.

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The most potent known naturally occurring Bowman-Birk inhibitor, sunflower trypsin inhibitor-1 (SFTI-1), is a bicyclic 14-amino acid peptide from sunflower seeds comprising one disulfide bond and a cyclic backbone. At present, little is known about the cyclization mechanism of SFTI-1. We show here that an acyclic permutant of SFTI-1 open at its scissile bond, SFTI-1[ 6,5], also functions as an inhibitor of trypsin and that it can be enzymatically backbone-cyclized by incubation with bovine beta-trypsin. The resulting ratio of cyclic SFTI-1 to SFTI1[6,5] is similar to9:1 regardless of whether trypsin is incubated with SFTI-1[ 6,5] or SFTI-1. Enzymatic resynthesis of the scissile bond to form cyclic SFTI-1 is a novel mechanism of cyclization of SFTI-1[ 6,5]. Such a reaction could potentially occur on a trypsin affinity column as used in the original isolation procedure of SFTI-1. We therefore extracted SFTI-1 from sunflower seeds without a trypsin purification step and confirmed that the backbone of SFTI-1 is indeed naturally cyclic. Structural studies on SFTI-1[ 6,5] revealed high heterogeneity, and multiple species of SFTI-1[ 6,5] were identified. The main species closely resembles the structure of cyclic SFTI-1 with the broken binding loop able to rotate between a cis/trans geometry of the I7-P8 bond with the cis conformer being similar to the canonical binding loop conformation. The non-reactive loop adopts a beta-hairpin structure as in cyclic wild-type SFTI-1. Another species exhibits an isoaspartate residue at position 14 and provides implications for possible in vivo cyclization mechanisms.

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Microcin J25 is a 21 amino acid bacterial peptide that has potent antibacterial activity against Gram-negative bacteria, resulting from its interaction with RNA polymerase. The peptide was previously proposed to have a head-to-tail cyclized peptide backbone and a tight globular structure (Blond, A., Peduzzi, J., Goulard, C., Chiuchiolo, M. J., Barthelemy, M., Prigent, Y., Salomon, R. A., Farias, R. N., Moreno, F. & Rebuffat, S. Eur. J. Biochem. 1999, 259, 747-755). It exhibits remarkable thermal stability for a peptide of its size lacking disulfide bonds and in part this was previously proposed to derive from its macrocyclic structure. We show here that in fact the peptide does not have a head-to-tail cyclic structure but rather a side chain to backbone cyclization between Glu8 and the N-terminus. This creates an embedded ring that is threaded by the C-terminal tail of the molecule, forming a noose-like feature. The three-dimensional structure deduced from NMR data suggests that slippage of the noose is prevented by two aromatic residues flanking the embedded ring. Unthreading does not occur even when the molecule is enzymatically digested with thermolysin. The new structural interpretation fully accounts for previously reported NMR and biophysical data and is consistent with the remarkable stability of this potent antimicrobial peptide.

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In recent years an increasing number of miniproteins containing an amide-cyclized backbone have been discovered. The cyclotide family is the largest group of such proteins and is characterized by a circular protein backbone and six conserved cysteine residues linked by disulfide bonds in a tight core of the molecule. These form a cystine knot in which an embedded ring formed by two of the disulfide bonds and the connecting backbone segment is threaded by a third disulfide bond. In the current study we have undertaken high resolution structural analysis of two prototypic cyclotides, kalata B1 and cycloviolacin O1, to define the role of the conserved residues in the sequence. We provide the first comprehensive analysis of the topological features in this unique family of proteins, namely rings (a circular backbone), twists (a cis-peptide bond in the Mobius cyclotides) and knots (a knotted arrangement of the disulfide bonds).