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Titlebook: Dynamics and the Problem of Recognition in Biological Macromolecules; Oleg Jardetzky,Jean-Fran?ois Lefèvre Book 1996 Springer Science+Busi

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發(fā)表于 2025-3-21 16:29:53 | 只看該作者 |倒序?yàn)g覽 |閱讀模式
書目名稱Dynamics and the Problem of Recognition in Biological Macromolecules
編輯Oleg Jardetzky,Jean-Fran?ois Lefèvre
視頻videohttp://file.papertrans.cn/284/283986/283986.mp4
叢書名稱NATO Science Series A:
圖書封面Titlebook: Dynamics and the Problem of Recognition in Biological Macromolecules;  Oleg Jardetzky,Jean-Fran?ois Lefèvre Book 1996 Springer Science+Busi
描述From within complex structures of organisms and cells down to the molecular level, biological processes all involve movement. Muscular fibers slide on each other to activate the muscle, as polymerases do along nucleic acids for replicating and transcribing the genetic material. Cells move and organize themselves into organs by recognizing each other through macromolecular surface-specific interactions. These recognition processes involve the mu- tual adaptation of structures that rely on their flexibility. All sorts of conformational changes occur in proteins involved in through-membrane signal transmission, showing another aspect of the flexibility of these macromolecules. The movement and flexibility are inscribed in the polymeric nature of essential biological macromolecules such as proteins and nucleic acids. For instance, the well-defined structures formed by the long protein chain are held together by weak noncovalent interac- tions that design a complex potential well in which the protein floats, permanently fluctuating between several micro- or macroconformations in a wide range of frequencies and ampli- tudes. The inherent mobility of biomolecular edifices may be crucial t
出版日期Book 1996
關(guān)鍵詞DNA; DNA double helix; cells; polymer; protein; proteins; spectroscopy
版次1
doihttps://doi.org/10.1007/978-1-4615-5839-2
isbn_softcover978-1-4613-7677-4
isbn_ebook978-1-4615-5839-2
copyrightSpringer Science+Business Media New York 1996
The information of publication is updating

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The Direct Determination of Protein Structure from Multidimensional NMR Spectra without Assignment,the implications and the problems that need to be overcome for the application of the approach and we suggest that some of the approaches to the interpretation of data used in X-ray crystallography may find parallels in the determination of structures by NMR.
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Approaches to the Determination of More Accurate Cross-Relaxation Rates and the Effects of Improvedand a macromolecular NOESY dataset may contain thousands of such peaks. Typically, each assigned cross peak is used to derive a distance “constraint,” or pair of bounds between which the distance is assumed to lie, and the dataset of bounds (perhaps along with additional information) is fed into one
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Heteronuclear Relaxation and the Experimental Determination of the Spectral Density Function,on & Harvey, 1985; Brooks et al., 1988). Understanding such motion inside a protein might thus provide some insight into their behavior. For example, it may allow the elucidation of the potential energy surface on which these proteins move, it may provide some clues on how they fold from a linear ch
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Simulating the Dynamics of the DNA Double Helix in Solution,biologically important state, are of dodecamer or decamer double-helical sequences. 29 of the 31 dodecamers pack in exactly the same way found originally by Drew et al. (1981) and show more disorder than seen in most protein crystals (resolution ranges from 1.9 ? to 3 ?). In fact, even at very low t
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Developments in NMR Structure Determination of Nucleic Acids,niques X-ray crystallography and NMR spectroscopy. It has been found, however, that in these molecules particular regions may adopt highly intricate folding patterns which are functionally very important. Examples are the ribozyme [Pley et al. (1994); Scott et al., (1995)] and pseudoknot motifs in R
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Solution Dynamics of the ,-Repressor Studied by NMR Spectroscopy,fetime of exchange ranging from millisecond to seconds and hours) can be investigated by techniques such as magnetization transfer, isotope replacement and lineshape analysis. The question therefore arises: How are the motions detected by NMR related to motions that are essential for function?
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