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Titlebook: Neutrons in Biology; Benno P. Schoenborn Book 1984 Springer Science+Business Media New York 1984 life sciences

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发表于 2025-3-21 16:38:28 | 显示全部楼层 |阅读模式
书目名称Neutrons in Biology
编辑Benno P. Schoenborn
视频video
丛书名称Basic Life Sciences
图书封面Titlebook: Neutrons in Biology;  Benno P. Schoenborn Book 1984 Springer Science+Business Media New York 1984 life sciences
出版日期Book 1984
关键词life sciences
版次1
doihttps://doi.org/10.1007/978-1-4899-0375-4
isbn_softcover978-1-4899-0377-8
isbn_ebook978-1-4899-0375-4
copyrightSpringer Science+Business Media New York 1984
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发表于 2025-3-21 22:27:31 | 显示全部楼层
Structural Elements of the 50 S Subunit of , Ribosomeseither to an amino acid or to a processing signal for the ribosome. Most of the investigations concerning protein biosynthesis are performed on the ribosome of the bacterium . The main structural features of the . ribosome are summarized in Table 1.
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Neutron Optics with Multilayer Monochromatorsltilayers made of suitable materials can also be used as very efficient polarizers of neutrons. Mezei (6), Ebisawa et al. (1), and Scharpf (11) developed supermirrors by introducing a continuous variation in d-spacings of multilayers.
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Neutron Scattering and the 30 S Ribosomal Subunit of ,somes, whatever their source, to be two-subunit enzymes. It is most unlikely that mechanistic questions of even this simple kind will be answered until much more is known about the three-dimensional structure of these particles than is known today.
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Use of the Neutron Diffraction—H/D Exchange Technique to Determine the Conformational Dynamics of Treractions. Although most of these fluctuations probably have little direct effect on the regions responsible for functional activity of the protein, a growing body of evidence indicates that conformational change is an important ingredient in a significant number of biological processes (7–10).
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