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Titlebook: Dynamic Aspects of Conformation Changes in Biological Macromolecules; Proceedings of the 2 Charles Sadron (Professeur au Muséum National d’

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發(fā)表于 2025-3-21 17:50:11 | 只看該作者 |倒序瀏覽 |閱讀模式
書目名稱Dynamic Aspects of Conformation Changes in Biological Macromolecules
副標題Proceedings of the 2
編輯Charles Sadron (Professeur au Muséum National d’Hi
視頻videohttp://file.papertrans.cn/284/283513/283513.mp4
圖書封面Titlebook: Dynamic Aspects of Conformation Changes in Biological Macromolecules; Proceedings of the 2 Charles Sadron (Professeur au Muséum National d’
描述On the day after the 1959 Cambridge Congress, during which the International Union of Pure and Applied Biophysics was founded, a biophysics section was formed within the Society of Physical Chemistry (Societe de Chimie Physique). Since then, three of the Society‘s annual meetings (the 11th, 17th, and 23rd) were devoted exclusively to the physico-chemical study of biological systems. The first of these was held in June 1961 at a hotel in Col de Voza, at the foot of an alpine glacier above Chamonix. The second, in May 1967, took place in the more learned setting of the venerable rooms of the National Museum of Natural History in Paris. The third - the one dealt with in the present volume - was recently held at Orleans-La Source in the newly built lecture theatres of the young University, which is near the great Institutes of the National Centre for Scientific Research (CNRS), on the Sologne plateau. These three stages are milestones of an evolution which characterises (at least schematically) the explosive evolution of biological physico-chemistry. The first colloquium, with the title ‘Deoxyribonucleic Acid: Structure, Synthesis and Functions‘, actually marks the first contact of the
出版日期Conference proceedings 1973
關鍵詞Diffusion; NMR; fluorescence; isotope; physical chemistry; structure
版次1
doihttps://doi.org/10.1007/978-94-010-2579-9
isbn_softcover978-94-010-2581-2
isbn_ebook978-94-010-2579-9
copyrightD. Reidel Publishing Company, Dordrecht, Holland 1973
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978-94-010-2581-2D. Reidel Publishing Company, Dordrecht, Holland 1973
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地板
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https://doi.org/10.1007/978-3-322-86690-5ed and partially oxidized forms. Comparison of these structures is beginning to show the conformational changes involved in the cooperative binding of oxygen to hemoglobin. This paper will attempt to summarize the data at hand and indicate where the missing structural information can be found.
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Die optimale Organisation Ihrer Arbeitparately, quantum-mechanical methods enable the evaluation of the total molecular energy of a molecular system corresponding to any given configuration of the constituent atoms. The author describes the results of a quantum-mechanical calculation on the conformational properties of the amino-acid re
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Eine gute Gliederung — die halbe Mietenant bien connu. Il a néanmoins semblé utile d’en faire une mise au point pour montrer notamment comment on peut justifier la décomposition de l’énergie potentielle d’interaction moléculaire en plusieurs termes. Il est intéressant de constater qu’aux minimums de l’énergie d’interaction de Van der Wa
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Die optimale Organisation Ihrer Arbeits donnerons quelques exemples de l’influence des caractéristiques cinétiques du repliement de la cha?ne polypeptidique sur l’état atteint après ‘renaturation’. Ces exemples, ainsi que l’effet de divers cofacteurs sur la restructuration de protéines dénaturées, indiquent que les propriétés cinétiques
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https://doi.org/10.1007/978-3-322-86690-5ounds, in which the number of conformations and hence the variety of vicinal interactions are very greatly reduced..In this communication we wish to report some results obtained with oligo-.-ethyl-L-glutamates, oligo-L-isoleucines, and oligo-L-phenylalanines..A combination of modern techniques and i
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Politikwissenschaft. Ein überblickatoms, and the approach of the solution towards isotopic equilibrium (the ‘relaxation’) is observed. The measured relaxation times of the isotopic exchange of peptide hydrogen atoms in protein solutions are much longer than the corresponding relaxation times in solutions of randomly coiled polypepti
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