東華大學圖書館 |

語系: 繁體中文

說明(常見問題)

回圖書館首頁

手機版館藏查詢

登入

回首頁

切換: 標籤 | MARC模式 | ISBD

Fundamentals and applications of nan...

Tessier, Peter Matthew.

FindBook

Google Book

Amazon

博客來

Fundamentals and applications of nanoparticle interactions and self-assembly.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Fundamentals and applications of nanoparticle interactions and self-assembly./
作者:	Tessier, Peter Matthew.
面頁冊數:	267 p.
附註:	Source: Dissertation Abstracts International, Volume: 64-08, Section: B, page: 3943.
Contained By:	Dissertation Abstracts International64-08B.
標題:	Engineering, Chemical. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3100125
ISBN:	0496477165

Fundamentals and applications of nanoparticle interactions and self-assembly.
Tessier, Peter Matthew.

Fundamentals and applications of nanoparticle interactions and self-assembly. - 267 p.

Source: Dissertation Abstracts International, Volume: 64-08, Section: B, page: 3943.

Thesis (Ph.D.)--University of Delaware, 2003.

The subject of this thesis is the development and implementation of novel methods for measuring colloidal interactions, and the elucidation of how these interactions influence a variety of separation and assembly processes. Weak interactions between nanometer-sized particles can be measured by colloidal characterization techniques such as static light scattering. Two novel alternative methods, self-interaction chromatography and self-interaction nanoparticle spectroscopy, were developed to characterize weak protein interactions. Both techniques yielded measurements comparable to osmotic second virial coefficients obtained by light scattering for several proteins, but the self-interaction techniques are appreciably more efficient. These high-throughput screening tools were used to investigate the interaction behavior of several proteins that have proven difficult to crystallize previously. The extensive set of virial coefficients revealed a variety of surprising trends that provided important insights into previous difficulties in crystallizing these proteins. The corresponding phase behavior experiments confirmed previous findings that, in general, solution conditions conducive to crystallization correspond to weakly attractive interactions. Most importantly, a methodology for crystallizing proteins in a rational manner was demonstrated that should be applicable to proteins that have not been crystallized previously.

ISBN: 0496477165Subjects--Topical Terms:

1018531
Engineering, Chemical.

Fundamentals and applications of nanoparticle interactions and self-assembly.
LDR:03624nmm 2200313 4500 001 1837243
005 20050428085947.5
008 130614s2003 eng d
020 $a 0496477165
035 $a (UnM)AAI3100125
035 $a AAI3100125
040 $a UnM $c UnM
100 1 $a Tessier, Peter Matthew. $3 1925697
245 1 0 $a Fundamentals and applications of nanoparticle interactions and self-assembly.
300 $a 267 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-08, Section: B, page: 3943.
500 $a Professors in charge: Abraham M. Lenhoff; Stanley I. Sandler.
502 $a Thesis (Ph.D.)--University of Delaware, 2003.
520 $a The subject of this thesis is the development and implementation of novel methods for measuring colloidal interactions, and the elucidation of how these interactions influence a variety of separation and assembly processes. Weak interactions between nanometer-sized particles can be measured by colloidal characterization techniques such as static light scattering. Two novel alternative methods, self-interaction chromatography and self-interaction nanoparticle spectroscopy, were developed to characterize weak protein interactions. Both techniques yielded measurements comparable to osmotic second virial coefficients obtained by light scattering for several proteins, but the self-interaction techniques are appreciably more efficient. These high-throughput screening tools were used to investigate the interaction behavior of several proteins that have proven difficult to crystallize previously. The extensive set of virial coefficients revealed a variety of surprising trends that provided important insights into previous difficulties in crystallizing these proteins. The corresponding phase behavior experiments confirmed previous findings that, in general, solution conditions conducive to crystallization correspond to weakly attractive interactions. Most importantly, a methodology for crystallizing proteins in a rational manner was demonstrated that should be applicable to proteins that have not been crystallized previously.
520 $a Self-interaction chromatography can also be adapted to measure protein cross-interactions directly. Virial cross coefficients measured for several model systems agreed with the small number of values in the literature.{09}The cross coefficient measurements were also found to correlate with diafiltration measurements for lysozyme in the presence of BSA using a membrane that was permeable only to lysozyme; when the cross-interactions were most attractive, the transmission of lysozyme was lowest, and vice versa.
520 $a Finally, the templated assembly of gold nanoparticles by latex microspheres was investigated as a method of synthesizing a new class of porous metallic materials. Colloidal crystals were assembled and backfilled with gold nanoparticles. The colloidal crystals could then be removed, producing a porous gold structure. The gold films possessed intriguing optical properties, and showed high sensitivity as surface-enhanced Raman spectroscopy substrates when used to detect several model compounds. This sensitivity was comparable to that of the best results achieved previously, although the films in this work were fabricated in a simpler and less expensive manner.
590 $a School code: 0060.
650 4 $a Engineering, Chemical. $3 1018531
650 4 $a Biophysics, General. $3 1019105
690 $a 0542
690 $a 0786
710 2 0 $a University of Delaware. $3 1017826
773 0 $t Dissertation Abstracts International $g 64-08B.
790 1 0 $a Lenhoff, Abraham M., $e advisor
790 1 0 $a Sandler, Stanley I., $e advisor
790 $a 0060
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3100125