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Titlebook: Mechanisms of Protein Synthesis; Structure-Function R Engin Bermek Conference proceedings 1985 Springer-Verlag, Berlin Heidelberg 1985 mole

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書(shū)目名稱(chēng)Mechanisms of Protein Synthesis
副標(biāo)題Structure-Function R
編輯Engin Bermek
視頻videohttp://file.papertrans.cn/629/628757/628757.mp4
叢書(shū)名稱(chēng)Proceedings in Life Sciences
圖書(shū)封面Titlebook: Mechanisms of Protein Synthesis; Structure-Function R Engin Bermek Conference proceedings 1985 Springer-Verlag, Berlin Heidelberg 1985 mole
描述This volume contains the papers presented at the international symposium on "Molecular Mechanisms in Protein Synthesis" held on September 26-27, 1983 at the Beyaz Ko§k in Emirgan, Bosphorus, Istanbul. The symposium aimed to create a medium for information exchange and discussions regarding the current developments in the area of protein syn- thesis. To ensure an informal yet scientifically stimulating and productive atmosphere providing opportunity for relaxed and speculative discussions, the number of presentations was limited to twenty and that of attendants to about sixty. The emphasis in the symposium was laid on structure-function relations in the prokaryotic protein synthesizing systems and on the control mechanisms of eukaryotic protein synthesis, in particular, during chain initia- tion. Other issues like evolutionary aspects of protein synthesis, translational components genes and proofreading were covered as well. The manuscripts represent the extended accounts of the oral presenta- tions, and it has been aimed with the concluding remarks at the end of the volume to give a summarizing view of the presentations and the discussions.
出版日期Conference proceedings 1985
關(guān)鍵詞molecular mechanisms; protein; protein synthesis; synthesis; translation
版次1
doihttps://doi.org/10.1007/978-3-642-69912-2
isbn_softcover978-3-642-69914-6
isbn_ebook978-3-642-69912-2Series ISSN 0172-6625
issn_series 0172-6625
copyrightSpringer-Verlag, Berlin Heidelberg 1985
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Ribosomal Components of the Peptidyl Transferase CenterNoller 1984, Wollenzien et al. 1984). Yet our understanding of the ribosomal mechanisms has remained rather fragmentary. The extremely complex interplay of the various factors involved in initiation, elongation, and termination, the interactions of mRNA and tRNA with the various ribosomal components
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tRNA Binding to and Topographical Arrangement on , Ribosomes molecules must be complemented by structural, thermodynamic, and kinetic information. Typically, this entails the use of physicochemical methods. The present contribution illustrates how fluorescence techniques can be used to study the mechanism of tRNA-ribosome complex formation and dissociation a
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Studies on Structural Dynamics of the Translating Ribosome binding, transpeptidation, and translocation (Watson 1964; Lipmann 1969). The translocation step includes significant intraribosomal displacements of a template and the products of the transpeptidation reaction: the release of deacylated tRNA, the transport of peptidyl-tRNA from one site to the oth
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The Effect of “In Vivo“ Incorporation of α-Aminobutyric Acid into , Proteins in different organisms (Uly and Wold 1977). Living organisms were not designed to use 20 primary amino acids; it evolved by random mutation. Since the rules of evolution remain the same now as always, i.e., nothing is immutable, it should be possible to force a cell to grow on an amino acid analog.
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