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Examination of protein adsorption wi...

Nsiah, Francis.

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Examination of protein adsorption with surface-sensitive spectroscopic techniques.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Examination of protein adsorption with surface-sensitive spectroscopic techniques./
作者:	Nsiah, Francis.
面頁冊數:	99 p.
附註:	Source: Masters Abstracts International, Volume: 42-02, page: 0596.
Contained By:	Masters Abstracts International42-02.
標題:	Chemistry, Organic. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoeng/servlet/advanced?query=MQ82321
ISBN:	0612823210

Examination of protein adsorption with surface-sensitive spectroscopic techniques.
Nsiah, Francis.

Examination of protein adsorption with surface-sensitive spectroscopic techniques. - 99 p.

Source: Masters Abstracts International, Volume: 42-02, page: 0596.

Thesis (M.Sc.)--University of Alberta (Canada), 2003.

In this thesis, infrared reflection absorption spectroscopy (IRRAS) and surface plasmon resonance (SPR) imaging were employed to explore adsorption characteristics of human fibrinogen (HFG) human fibronectin (HFN), bovine serum albumin (BSA) and lysozyme (LYS).

ISBN: 0612823210Subjects--Topical Terms:

516206
Chemistry, Organic.

Examination of protein adsorption with surface-sensitive spectroscopic techniques.
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245 1 0 $a Examination of protein adsorption with surface-sensitive spectroscopic techniques.
300 $a 99 p.
500 $a Source: Masters Abstracts International, Volume: 42-02, page: 0596.
500 $a Adviser: Mark T. McDermott.
502 $a Thesis (M.Sc.)--University of Alberta (Canada), 2003.
520 $a In this thesis, infrared reflection absorption spectroscopy (IRRAS) and surface plasmon resonance (SPR) imaging were employed to explore adsorption characteristics of human fibrinogen (HFG) human fibronectin (HFN), bovine serum albumin (BSA) and lysozyme (LYS).
520 $a Self-assembled monolayers (SAMs) on gold were used to control surface chemistry. The SAMs were characterized using IRRAS and contact angle measurements. Octadecanethiol (ODT) was used as a model neutral, hydrophobic surface. 16-mercapto-hexadecanoic acid (MHA) provides a hydrophilic, partially negatively charged surface at pH 7.4. CH<sub>2</sub>OH terminated monolayers of 11-mercapto-l-undecanol (MUL) was employed as a protein-resistant control surface. The differences in chemistries of the SAMs provided a platform to map variations in the amount of protein adsorbed and surface-induced protein conformation and/or orientation.
520 $a IRRAS was employed on single component monolayers to obtain information on surface coverage as well as on the adsorbed state of the proteins.
520 $a SPR imaging has been used for the first time as a means to visualized adsorbed state of proteins on patterned substrates. (Abstract shortened by UMI.)
590 $a School code: 0351.
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