By Lasse B. Jenner, Adam Ben-Shem (auth.), Jonathan D. Dinman (eds.)

ISBN-10: 1461439906

ISBN-13: 9781461439905

ISBN-10: 1461439914

ISBN-13: 9781461439912

This e-book presents a most appropriate source on realizing the ribosome's crucial nature and the way it interacts with different proteins and nucleic acids to manage protein synthesis. As one of many imperative foundations in our knowing of the biology on the molecular point, this subject appeals to a large viewers, from bench researcher to clinician. With the appearance of atomic scale buildings, tips on how to visualize and separate person molecules, and the computational energy to version the advanced interactions of over one million atoms instantaneously, our figuring out of ways gene expression is managed on the point of protein translation is now deeply ensconced within the biophysical realm.

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Biophysical approaches to translational control of gene by Lasse B. Jenner, Adam Ben-Shem (auth.), Jonathan D. Dinman PDF

This e-book offers a ultimate source on realizing the ribosome's crucial nature and the way it interacts with different proteins and nucleic acids to manage protein synthesis. As one of many principal foundations in our knowing of the biology on the molecular point, this subject appeals to a large viewers, from bench researcher to clinician.

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Extra resources for Biophysical approaches to translational control of gene expression

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Source: Fig “No. 7” from the following reference Datta et al. (2007) a h28 Era RbfA b Era RbfA h28 p h C h27 h1 bk b processed efficiently to 16S rRNA. Thus it was important to investigate how RbfA was working. Even after several try crystallization of 30S⋅RbfA was not possible by a Japanese research group (personal communication) which led Datta et al. (2007) to study the 30S⋅RbfA complex under cryo-EM. Analyses of the 30S⋅RbfA cryoEM map through molecular docking showed that RbfA bound to the 30S subunit in a position overlapping to the binding sites of the A- and P-site tRNAs, and RbfA’s functionally important C terminus extended toward the 5¢ end of the 16S rRNA, which could provide stability to form the canonical helix 1.

2007) a h28 Era RbfA b Era RbfA h28 p h C h27 h1 bk b processed efficiently to 16S rRNA. Thus it was important to investigate how RbfA was working. Even after several try crystallization of 30S⋅RbfA was not possible by a Japanese research group (personal communication) which led Datta et al. (2007) to study the 30S⋅RbfA complex under cryo-EM. Analyses of the 30S⋅RbfA cryoEM map through molecular docking showed that RbfA bound to the 30S subunit in a position overlapping to the binding sites of the A- and P-site tRNAs, and RbfA’s functionally important C terminus extended toward the 5¢ end of the 16S rRNA, which could provide stability to form the canonical helix 1.

Nature 389:403–406 Taylor DJ, Devkota B, Huang AD, Topf M, Narayanan E et al (2009) Comprehensive molecular structure of the eukaryotic ribosome. Structure 17:1591–1604 Urbonavicius J, Qian Q, Durand JM, Hagervall TG, Bjork GR (2001) Improvement of reading frame maintenance is a common function for several tRNA modifications. EMBO J 20:4863–4873 Urbonavicius J, Stahl G, Durand JM, Ben Salem SN, Qian Q et al (2003) Transfer RNA modifications that alter +1 frameshifting in general fail to affect −1 frameshifting.

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Biophysical approaches to translational control of gene expression by Lasse B. Jenner, Adam Ben-Shem (auth.), Jonathan D. Dinman (eds.)


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