國立高雄大學圖資館 |

Language: English

Back

Solution structure of ribosomal protein L18 from Bacillus stearothermophilus

Record Type:	Electronic resources : Monograph/item
Title/Author:	Solution structure of ribosomal protein L18 from Bacillus stearothermophilus
Author:	Turner, Catherine Filotto.
Description:	150 p.
Notes:	Director: Peter B. Moore.
Notes:	Source: Dissertation Abstracts International, Volume: 65-03, Section: B, page: 1313.
Contained By:	Dissertation Abstracts International65-03B.
Subject:	Chemistry, Biochemistry.
Online resource:	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
LDR:01689nmm _2200265 _450 001 162528
005 20051017073455.5
008 230606s2004 eng d
020 $a 0496726080
035 $a 00149029
035 $a 162528
040 $a UnM $c UnM
100 0 $a Turner, Catherine Filotto. $3 227670
245 1 0 $a Solution structure of ribosomal protein L18 from Bacillus stearothermophilus $h [electronic resource]
300 $a 150 p.
500 $a Director: Peter B. Moore.
500 $a Source: Dissertation Abstracts International, Volume: 65-03, Section: B, page: 1313.
502 $a Thesis (Ph.D.)--Yale University, 2004.
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.
590 $a School code: 0265.
650 # 0 $a Chemistry, Biochemistry. $3 226900
690 $a 0487
710 0 # $a Yale University. $3 212430
773 0 # $g 65-03B. $t Dissertation Abstracts International
790 $a 0265
790 1 0 $a Moore, Peter B., $e advisor
791 $a Ph.D.
792 $a 2004
856 4 0 $u http://libsw.nuk.edu.tw/login?url=http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3125318 $z http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3125318