Author: Viktor Stolc
Publisher:
ISBN:
Category :
Languages : en
Pages : 354

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Author: Joel Ranier Chamberlain
Publisher:
ISBN:
Category :
Languages : en
Pages : 348

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Author: Shaohua Xiao
Publisher:
ISBN:
Category :
Languages : en
Pages : 294

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Author: Yan Li Dang
Publisher:
ISBN:
Category :
Languages : en
Pages : 242

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Author: Anthony John Tranguch
Publisher:
ISBN:
Category :
Languages : en
Pages : 280

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Author: Fenyong Liu
Publisher: Springer Science & Business Media
ISBN: 1441911421
Category : Science
Languages : en
Pages : 293

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Book Description
The Discovery of Ribonuclease P and Enzymatic Activity of Its RNA Subunit Sydney Brenner and Francis H. C. Crick had a specific project in mind when they offered Sidney Altman a position in their group in 1969 to conduct postdoctoral research at the Medical Research Council Laboratory of Molecular Biology (LMB) in Cambridge, England. At the time, an intense international competition was on- ing in as many as a dozen labs to determine the three-dimensional structure of tRNA. At the LMB, Aaron Klug was attacking the structure by crystallographic analysis with Brian F. C. Clark providing large amounts of purified phenylalanine tRNA. (Eventually, Aaron announced his empirically determined 3-D structure of yeast phenylalanine tRNA, a structure that is generally common to tRNAs, due in part to several conserved, novel three-way nucleotide interactions. ) Concurrently, Michael Levitt, a Ph. D. student of Francis, was visually scrutinizing the cloverleaf secondary structure of the 14 tRNA sequences known at the time. Levitt was searching for nucleotide covariation in different parts of the molecules that were conserved in the 14 sequences known at the time. He identified a possible covariation of an apparent Watson-Crick pairing type between the residues at position 15 from the 5’ end of the tRNA and residue 48. This association implied these parts of the tRNA, namely the D loop containing residue 15 and the 5’ end of the T stem-adjoining residue 48, folded on one another in a tertiary structure shared by different tRNAs.

Author: JAE-YONG LEE
Publisher:
ISBN:
Category :
Languages : en
Pages : 144

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Mg$\sp{++}$ is associated with RNase P to constitute an active enzyme and that the protein subunits of S. cerevisiae nuclear RNase P may be involved in catalysis.

Author:
Publisher:
ISBN:
Category : Dissertations, Academic
Languages : en
Pages : 942

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Author: M.R. El-Gewely
Publisher: Elsevier
ISBN: 008087732X
Category : Science
Languages : en
Pages : 497

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Book Description
The Biotechnology Annual Review covers the various developments in biotechnology in the form of comprehensive, illustrated and well referenced reviews. With the expansion of the field of biotechnology, coupled with the vast increase in the number of new journals reporting recent results in this field, the need for a publication that is continuously providing reviews is urgent. Hence, each volume of the Biotechnology Annual Review will have a number of reviews covering different aspects of biotechnology. Reviewed topics will include biotechnology applications in medicine, agriculture, marine biology, industry, bioremedation and the environment. Fundamental problems dealing with enhancing the technical knowledge encountering biotechnology utilization regardless of the field of application will be particularly emphasized. This series will help both students and teachers, researchers as well as administrators to remain knowledgeable on all relevant issues in biotechnology.Proposals for contributions and/or suggestions for topics for future volumes in this series should be sent to the Editor:professor M.R. El-GewelyDepartment of BiotechnologyUniversity of TromsløIMB, MH-ByggetN-9037 TromsøNorwayTel: (+47) 77 644000Fax: (+47) 77 645350

Author: Robert J. White
Publisher: Springer Science & Business Media
ISBN: 3662035189
Category : Science
Languages : en
Pages : 274

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Book Description
This monograph reviews and summarizes the substantial body of work that has been published on the transcription by polymerase III over the past 5 years. Progress in this field has been very rapid since 1993, and this new edition incorporates all the recent developments and offers the reader a highly detailed analysis of the current state of research on this largest and most complex of the eukaryotic RNA polymerases.