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Small-angle X-ray scattering of RNA,...

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Small-angle X-ray scattering of RNA, proteins, and membrane protein-detergent complexes.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Small-angle X-ray scattering of RNA, proteins, and membrane protein-detergent complexes./
Author:	Lipfert, Jan.
Description:	195 p.
Notes:	Adviser: Sebastian Doniach.
Contained By:	Dissertation Abstracts International68-12B.
Subject:	Biology, Molecular. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=3292388
ISBN:	9780549355236

Small-angle X-ray scattering of RNA, proteins, and membrane protein-detergent complexes.
Lipfert, Jan.

Small-angle X-ray scattering of RNA, proteins, and membrane protein-detergent complexes. - 195 p.

Adviser: Sebastian Doniach.

Thesis (Ph.D.)--Stanford University, 2008.

This thesis describes applications of the small-angle X-ray scattering (SAXS) technique to biological macromolecules, viz. peptides, (membrane) proteins, and nucleic acids. In a typical SAXS experiment, a sample volume of the molecule(s) of interest in solution is placed into an intense X-ray beam and the scattered intensity is recorded as a function of scattering angle. Being a solution scattering technique, SAXS can be readily applied to a diverse range of macromolecules under varied solution conditions. The resulting scattering profile provides information about the structure and interactions of macromolecules in solution, with a typical resolution on the order of 1 nm.

ISBN: 9780549355236Subjects--Topical Terms:

1017719
Biology, Molecular.

Small-angle X-ray scattering of RNA, proteins, and membrane protein-detergent complexes.
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008 100709s2008 ||||||||||||||||| ||eng d
020 $a 9780549355236
035 $a (UMI)AAI3292388
035 $a AAI3292388
040 $a UMI $c UMI
100 1 $a Lipfert, Jan. $3 1023431
245 1 0 $a Small-angle X-ray scattering of RNA, proteins, and membrane protein-detergent complexes.
300 $a 195 p.
500 $a Adviser: Sebastian Doniach.
500 $a Source: Dissertation Abstracts International, Volume: 68-12, Section: B, page: 7865.
502 $a Thesis (Ph.D.)--Stanford University, 2008.
520 $a This thesis describes applications of the small-angle X-ray scattering (SAXS) technique to biological macromolecules, viz. peptides, (membrane) proteins, and nucleic acids. In a typical SAXS experiment, a sample volume of the molecule(s) of interest in solution is placed into an intense X-ray beam and the scattered intensity is recorded as a function of scattering angle. Being a solution scattering technique, SAXS can be readily applied to a diverse range of macromolecules under varied solution conditions. The resulting scattering profile provides information about the structure and interactions of macromolecules in solution, with a typical resolution on the order of 1 nm.
520 $a The macromolecules discussed in this thesis, membrane proteins and detergent micelles, unfolded and partially folded proteins and peptides, and RNA, pose unique difficulties to standard techniques in structural biology. I show that SAXS is well suited to study these classes of molecules and that SAXS measurements can provide insight into their low resolution solution structure and into the forces that modulate their conformations.
520 $a There are four major sections in this thesis. Chapter 1 gives an introduction to SAXS and reviews recent trends and applications. Chapter 2 describes the design of a sample cell and sample holder, which was used at beam line 12-ID of the Advanced Photon Source for all SAXS experiments reported in this thesis. The second section comprises Chapters 2, 3, and 4 and reports on applications of SAXS to detergent micelles and membrane-protein detergent complexes. Chapter 6 illustrates how SAXS can be used to probe unfolded and partially folded peptides and reports on findings on the short, 11-residue peptide "XAO". The final section describes applications of SAXS to RNA. In Chapter 7, I show that ab initio structure reconstruction algorithms developed for proteins can be applied successfully to RNA. These algorithms permit to obtain low resolution 3D electron density maps from SAXS data. Chapter 8 describes how SAXS is used to study the conformations of a glycine-binding riboswitch as a function of glycine and Mg2+ concentration, and how shape reconstruction algorithms provide a first glimpse into the solution structure of this riboswitch.
590 $a School code: 0212.
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Biophysics, General. $3 1019105
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0307
690 $a 0487
690 $a 0786
710 2 $a Stanford University. $3 754827
773 0 $t Dissertation Abstracts International $g 68-12B.
790 $a 0212
790 1 0 $a Doniach, Sebastian, $e advisor
791 $a Ph.D.
792 $a 2008
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=3292388