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Solution structure of ribosomal protein L18 from Bacillus stearothermophilus

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Solution structure of ribosomal protein L18 from Bacillus stearothermophilus
作者:	Turner, Catherine Filotto.
面頁冊數:	150 p.
附註:	Director: Peter B. Moore.
附註:	Source: Dissertation Abstracts International, Volume: 65-03, Section: B, page: 1313.
Contained By:	Dissertation Abstracts International65-03B.
標題:	Chemistry, Biochemistry.
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3125318
ISBN:	0496726080

Solution structure of ribosomal protein L18 from Bacillus stearothermophilus
Turner, Catherine Filotto.

Solution structure of ribosomal protein L18 from Bacillus stearothermophilus [electronic resource] - 150 p.

Director: Peter B. Moore.

Thesis (Ph.D.)--Yale University, 2004.

A medium resolution structure has been obtained for L18 from Bacillus stearothermophilus (BstL18), a large ribosomal subunit protein that stabilizes the tertiary structure of 5S rRNA and mediates its interaction with the rest of the subunit. BstL18 has a globular domain consisting of a three-strand beta-sheet and two alpha-helices, a short fourth beta-strand, and an unstructured N-terminal tail. Its topology is the same as that of the other L18s of known structure, but the relative orientation of its alpha-helices and its beta-sheet is not. Nevertheless, modeling studies indicate that this conformational difference is unlikely to prevent BstL18 from performing the same function as other L18s in the ribosome.

ISBN: 0496726080Subjects--Topical Terms:

226900
Chemistry, Biochemistry.

Solution structure of ribosomal protein L18 from Bacillus stearothermophilus
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520 # $a A medium resolution structure has been obtained for L18 from Bacillus stearothermophilus (BstL18), a large ribosomal subunit protein that stabilizes the tertiary structure of 5S rRNA and mediates its interaction with the rest of the subunit. BstL18 has a globular domain consisting of a three-strand beta-sheet and two alpha-helices, a short fourth beta-strand, and an unstructured N-terminal tail. Its topology is the same as that of the other L18s of known structure, but the relative orientation of its alpha-helices and its beta-sheet is not. Nevertheless, modeling studies indicate that this conformational difference is unlikely to prevent BstL18 from performing the same function as other L18s in the ribosome.
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