873 resultados para University of Michigan. College of Literature, Science and the Arts
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"The Collapse of German Democracy and the Expansion of National Socialism" (1940):; 1. Darstellung des Forschungsprojekts (15.9.1940), b. Typoskript mit handschriftlichen Korrekturen, 78 Blatt; 2. "Research work on recent trends in the history of ideas (parts of the Research project on the Collapse of German Democracy would be included)". Als Memorandum zur Eröffnung zur Eröffnung einer Zweigstelle des Instituts in Los Angeles (12.12.1940): a) Typoskript, 2 Blatt, b) Teilstück, Typoskript mit handschriftlichen Korrekturen, 1 Blatt, c) Teilstück, Typoskript mit handschriftlichen Korrekturen, 1 Blatt, d) Teilstück, Typoskript, 1 Blatt, e) Teilstück, Typoskript, 1 Blatt, f) Entwurf, Typoskript mit handschriftlichen Korrekturen und Manuskript, 3 Blatt; 3. University of California, Los Angeles: 2 Briefe (Abschrift) von Max Horkheimer, o.O., 1940, 2 Briefe (Abschrift) an Max Horkheimer, 1940, 2 Blatt; A.R.L. Gurland: "Survey of Structural Changes in the German Economy, 1933 to 1939. Technological Bases and Organizational Forms of the National Socialist Economic System". Typoskript mit handschriftlichen Korrekturen unter anderem von Theodor W. Adorno, 48 Blatt (formal nicht identisch mit "Technological Trends and Economic Structure under National Socialism", Studies in Philosophy and Social Science, Bd. IX, 1941, S. 226ff.); "Cultural Aspects of National Socialism. A Research Project" (1941):; 1. Institute of Social Research: Mitteilung über das Forschungsprojekt und das 'Supplementary Statement', Typoskript, englisch, 4 Blatt; 2. Supplementary Statement to the Research Project, a) Typoskript, 14.4.1941, 63 Blatt, b) Typoskript, 12.4.1941, mit handschriftlichen Korrekturen, 35 Blatt; 3. "Cultural Aspects of National Socialism. A Research Project" (24.2.1941), a) als Typoskript vervielfältigt, 54 Blatt, b) Typoskript mit handschriftlichen Korrekturen, 34 Blatt, c) Fassung Januar 1941, Typoskript mit handschriftlichen Korrekturen, 40 Blatt; 4. Inhaltsverzeichnisse, mit handschriftlichen Korrekturen, 3 Blatt;
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Background: Octopods have successfully colonised the world's oceans from the tropics to the poles. Yet, successful persistence in these habitats has required adaptations of their advanced physiological apparatus to compensate impaired oxygen supply. Their oxygen transporter haemocyanin plays a major role in cold tolerance and accordingly has undergone functional modifications to sustain oxygen release at sub-zero temperatures. However, it remains unknown how molecular properties evolved to explain the observed functional adaptations. We thus aimed to assess whether natural selection affected molecular and structural properties of haemocyanin that explains temperature adaptation in octopods. Results: Analysis of 239 partial sequences of the haemocyanin functional units (FU) f and g of 28 octopod species of polar, temperate, subtropical and tropical origin revealed natural selection was acting primarily on charge properties of surface residues. Polar octopods contained haemocyanins with higher net surface charge due to decreased glutamic acid content and higher numbers of basic amino acids. Within the analysed partial sequences, positive selection was present at site 2545, positioned between the active copper binding centre and the FU g surface. At this site, methionine was the dominant amino acid in polar octopods and leucine was dominant in tropical octopods. Sites directly involved in oxygen binding or quaternary interactions were highly conserved within the analysed sequence. Conclusions: This study has provided the first insight into molecular and structural mechanisms that have enabled octopods to sustain oxygen supply from polar to tropical conditions. Our findings imply modulation of oxygen binding via charge-charge interaction at the protein surface, which stabilize quaternary interactions among functional units to reduce detrimental effects of high pH on venous oxygen release. Of the observed partial haemocyanin sequence, residue 2545 formed a close link between the FU g surface and the active centre, suggesting a role as allosteric binding site. The prevalence of methionine at this site in polar octopods, implies regulation of oxygen affinity via increased sensitivity to allosteric metal binding. High sequence conservation of sites directly involved in oxygen binding indicates that functional modifications of octopod haemocyanin rather occur via more subtle mechanisms, as observed in this study.
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v.38:pt.2 (1958)
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v.17 (1927)
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v.14 (1922)
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v.4 (1907-1908)
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v.5 (1909-1911)
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v.3 (1905-1906)
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v.2 (1903-1904)
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v.40 (1960)
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v.39 (1958)
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v.37:pt.1 (1955)
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v.46:no.13-22 (1966-1967)