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Titlebook: Chemical Relaxation in Molecular Biology; Israel Pecht,Rudolf Rigler Book 1977 Springer-Verlag Berlin · Heidelberg 1977 Molekularbiologie.

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书目名称Chemical Relaxation in Molecular Biology
编辑Israel Pecht,Rudolf Rigler
视频video
丛书名称Molecular Biology, Biochemistry and Biophysics‘ Molekularbiologie, Biochemie und Biophysik
图书封面Titlebook: Chemical Relaxation in Molecular Biology;  Israel Pecht,Rudolf Rigler Book 1977 Springer-Verlag Berlin · Heidelberg 1977 Molekularbiologie.
描述The development of an area of scientific research is a dynamic process with its own kinetic equations and its own physical mech­ anism. The study of fast chemical interactions and transformations is such an area, and while it is tempting to draw analogies or to speculate about the simplest model system, the lack of ade­ quately averaged observables is an annoying obstacle to such an undertaking. Sciences suffering from such conditions usually avoid quantitative models, be they primitive or complex. Instead, they prove their point by "case histories". Chemical relaxation kinetics started as an offspring of research in acoustics. In some aqueous ionic solutions anomalous acoustic absorption had been observed. A systematic study traced the cause of this absorption, showing that the covered frequency range and the intensity of the absorption were related in a predictable manner to the rate at which ions can interact and form structures differing in volume from the non interacting species. The step from this experimental observation and its correct, non­ trivial explanation to the discovery that all fast chemical pro­ cesses must reveal themselves quantitatively in the relaxation rate o
出版日期Book 1977
关键词Molekularbiologie; Relaxation; biology; development; molecular biology
版次1
doihttps://doi.org/10.1007/978-3-642-81117-3
isbn_softcover978-3-642-81119-7
isbn_ebook978-3-642-81117-3Series ISSN 0077-0221
issn_series 0077-0221
copyrightSpringer-Verlag Berlin · Heidelberg 1977
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Protein Folding and Unfolding,l. The determination of the spatial arrangement of the peptide chain by X-ray diffraction has given the most important information on the static properties of globular proteins. But the elucidation of the pathways of folding, the magnitude of the different thermodynamic forces involed, and the kinet
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