Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Albion E"'
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 2000 Apr 01. 97(8), 3954-3958.
Externí odkaz:
https://www.jstor.org/stable/122090
Akademický článek
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Publikováno v:
Journal of Molecular Biology. 354:459-472
We have used Förster resonance energy transfer (FRET) to study specific conformational changes in the Escherichia coli 30 S ribosomal subunit that occur upon association with the 50 S subunit. By measuring energy transfer between 13 different pairs
Autor:
Albion E. Baucom, Kathy Lieberman, Jamie H. D. Cate, Kurt Fredrick, Thomas Earnest, Harry F. Noller, Laura Lancaster, Anne Dallas, Gulnara Yusupova, Marat Yusupov
Publikováno v:
Cold Spring Harbor Symposia on Quantitative Biology. 66:57-66
Akademický článek
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Autor:
Harry F. Noller, Albion E. Baucom
Publikováno v:
Biochemical Society transactions. 30(Pt 6)
The ribosome is a complex molecular machine, with moving parts, many of which are structural elements of rRNA. We compared the X-ray crystal structures of three different functional states of the 30 S ribosomal subunit - two from crystal structures o
Publikováno v:
FEBS letters. 514(1)
Coupled translocation of tRNA and mRNA in the ribosome during protein synthesis is one of the most challenging and intriguing problems in the field of translation. We highlight several key questions regarding the mechanism of translocation, and discu
We have noted consistent structural similarities among unrelated proteases. In comparison with other proteins of similar size, proteases have smaller than average surface areas, smaller radii of gyration, and higher C α densities. These findings imp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7191c395516069f724c48b3b88b799f
https://europepmc.org/articles/PMC18123/
https://europepmc.org/articles/PMC18123/
Publikováno v:
Bioinformatics (Oxford, England). 15(4)
MOTIVATION: To facilitate the process of structure prediction by both comparative modeling and fold recognition, we describe DINAMO, an interactive protein alignment building and model evaluation tool that dynamically couples a multiple sequence alig