語系:
繁體中文
English
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
FindBook
Google Book
Amazon
博客來
Standing in the Way of Profiling Depth : = How the Selection of Chromatography and Mass Spectrometry Data Acquisition Limit Our View of the Proteome.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
Standing in the Way of Profiling Depth :/
其他題名:
How the Selection of Chromatography and Mass Spectrometry Data Acquisition Limit Our View of the Proteome.
作者:
Delafield, Daniel Graham.
面頁冊數:
1 online resource (493 pages)
附註:
Source: Dissertations Abstracts International, Volume: 84-10, Section: B.
Contained By:
Dissertations Abstracts International84-10B.
標題:
Chemistry. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=30425876click for full text (PQDT)
ISBN:
9798379440046
Standing in the Way of Profiling Depth : = How the Selection of Chromatography and Mass Spectrometry Data Acquisition Limit Our View of the Proteome.
Delafield, Daniel Graham.
Standing in the Way of Profiling Depth :
How the Selection of Chromatography and Mass Spectrometry Data Acquisition Limit Our View of the Proteome. - 1 online resource (493 pages)
Source: Dissertations Abstracts International, Volume: 84-10, Section: B.
Thesis (Ph.D.)--The University of Wisconsin - Madison, 2023.
Includes bibliographical references
This thesis outlines research focusing on the development and application of chromatography separation and mass spectrometry data acquisition methods aimed at improving profiling depth in proteomic analyses. This work is briefly outlined and explained in Chapter 1, highlighting how reliance on common analytical methodologies inherently limits our view of the proteome. Chapter 2 details the initial reports of utilizing porous graphitic carbon (PGC) chromatography as an alternative to reversed-phase liquid chromatography (RPLC). This report describes demonstrable improvements in peptide, glycopeptide, and protein identifications while highlighting the various analytical advantages seen over traditional separations. In this preliminary work, we observed elevated column temperatures imparted potentially detrimental effects of various glycopeptides, a phenomenon explored in Chapter 3. This following report provides heuristic guidance in PGC-based glycoproteomic analyses and details how column temperature must be optimized to suit the given analytical need. Chapter 4 provides a topical overview of quantitative approaches in glycan and glycopeptide analyses, providing meaningful consideration and comparison of methodologies most appropriate for use in future glycoproteomic analyses. In Chapter 5, we return to PGC separations with a specific focus on further detailing the benefits found in proteomic analyses. This report highlights substantial improvements in the number of peptide and protein identifications compared to what was seen previously and highlights the breadth of information lost during routine RPLC analyses. Chapter 6 departs from chromatographic separation and turns attention towards quantitative mass spectrometry (MS) methods useful for biological discovery. The knowledge and information garnered from this report informed the experimental design used in Chapter 7, which describes the employment of data independent acquisition (DIA)-MS to study a novel, progressive prostate cancer cell model. Here we quantified 6,614 proteins across 9 biological samples, finding 1,242 to be significantly dysregulated in malignant cancer phenotypes. These proteins demonstrate potential for disease diagnosis, phenotypic stratification, and therapeutic targeting. In Chapter 8 we expand on the utility of DIA-MS, detailing the ability to reuse and repurpose prior proteomic measurements for enhanced biomolecular identification. We apply this workflow to the analysis of neurological disorder patient cohorts, revealing 1,642 dysregulated proteins that speak to the biomolecular organization related to Alzheimer's Disease. Chapter 9 describes new and emerging ion mobility (IM)-based analytical modalities and discuss their capacity for biomolecular interrogation and structural analysis. Given instrumentation of this kind is not utilized in the works preceding, this report explains potential advantages and necessary considerations, should this technology become of interest. Finally, we conclude with Chapter 10, briefly discussing the various investigations that may follow this body of work.
Electronic reproduction.
Ann Arbor, Mich. :
ProQuest,
2023
Mode of access: World Wide Web
ISBN: 9798379440046Subjects--Topical Terms:
516420
Chemistry.
Subjects--Index Terms:
GlycoproteomicsIndex Terms--Genre/Form:
542853
Electronic books.
Standing in the Way of Profiling Depth : = How the Selection of Chromatography and Mass Spectrometry Data Acquisition Limit Our View of the Proteome.
LDR
:04611nmm a2200397K 4500
001
2363524
005
20231127093430.5
006
m o d
007
cr mn ---uuuuu
008
241011s2023 xx obm 000 0 eng d
020
$a
9798379440046
035
$a
(MiAaPQ)AAI30425876
035
$a
AAI30425876
040
$a
MiAaPQ
$b
eng
$c
MiAaPQ
$d
NTU
100
1
$a
Delafield, Daniel Graham.
$3
3704287
245
1 0
$a
Standing in the Way of Profiling Depth :
$b
How the Selection of Chromatography and Mass Spectrometry Data Acquisition Limit Our View of the Proteome.
264
0
$c
2023
300
$a
1 online resource (493 pages)
336
$a
text
$b
txt
$2
rdacontent
337
$a
computer
$b
c
$2
rdamedia
338
$a
online resource
$b
cr
$2
rdacarrier
500
$a
Source: Dissertations Abstracts International, Volume: 84-10, Section: B.
500
$a
Advisor: Li, Lingjun.
502
$a
Thesis (Ph.D.)--The University of Wisconsin - Madison, 2023.
504
$a
Includes bibliographical references
520
$a
This thesis outlines research focusing on the development and application of chromatography separation and mass spectrometry data acquisition methods aimed at improving profiling depth in proteomic analyses. This work is briefly outlined and explained in Chapter 1, highlighting how reliance on common analytical methodologies inherently limits our view of the proteome. Chapter 2 details the initial reports of utilizing porous graphitic carbon (PGC) chromatography as an alternative to reversed-phase liquid chromatography (RPLC). This report describes demonstrable improvements in peptide, glycopeptide, and protein identifications while highlighting the various analytical advantages seen over traditional separations. In this preliminary work, we observed elevated column temperatures imparted potentially detrimental effects of various glycopeptides, a phenomenon explored in Chapter 3. This following report provides heuristic guidance in PGC-based glycoproteomic analyses and details how column temperature must be optimized to suit the given analytical need. Chapter 4 provides a topical overview of quantitative approaches in glycan and glycopeptide analyses, providing meaningful consideration and comparison of methodologies most appropriate for use in future glycoproteomic analyses. In Chapter 5, we return to PGC separations with a specific focus on further detailing the benefits found in proteomic analyses. This report highlights substantial improvements in the number of peptide and protein identifications compared to what was seen previously and highlights the breadth of information lost during routine RPLC analyses. Chapter 6 departs from chromatographic separation and turns attention towards quantitative mass spectrometry (MS) methods useful for biological discovery. The knowledge and information garnered from this report informed the experimental design used in Chapter 7, which describes the employment of data independent acquisition (DIA)-MS to study a novel, progressive prostate cancer cell model. Here we quantified 6,614 proteins across 9 biological samples, finding 1,242 to be significantly dysregulated in malignant cancer phenotypes. These proteins demonstrate potential for disease diagnosis, phenotypic stratification, and therapeutic targeting. In Chapter 8 we expand on the utility of DIA-MS, detailing the ability to reuse and repurpose prior proteomic measurements for enhanced biomolecular identification. We apply this workflow to the analysis of neurological disorder patient cohorts, revealing 1,642 dysregulated proteins that speak to the biomolecular organization related to Alzheimer's Disease. Chapter 9 describes new and emerging ion mobility (IM)-based analytical modalities and discuss their capacity for biomolecular interrogation and structural analysis. Given instrumentation of this kind is not utilized in the works preceding, this report explains potential advantages and necessary considerations, should this technology become of interest. Finally, we conclude with Chapter 10, briefly discussing the various investigations that may follow this body of work.
533
$a
Electronic reproduction.
$b
Ann Arbor, Mich. :
$c
ProQuest,
$d
2023
538
$a
Mode of access: World Wide Web
650
4
$a
Chemistry.
$3
516420
650
4
$a
Analytical chemistry.
$3
3168300
653
$a
Glycoproteomics
653
$a
Liquid chromatography
653
$a
Mass spectrometry
653
$a
Proteomics
653
$a
Data independent acquisition
653
$a
Porous graphitic carbon
655
7
$a
Electronic books.
$2
lcsh
$3
542853
690
$a
0485
690
$a
0486
710
2
$a
ProQuest Information and Learning Co.
$3
783688
710
2
$a
The University of Wisconsin - Madison.
$b
Chemistry.
$3
2049906
773
0
$t
Dissertations Abstracts International
$g
84-10B.
856
4 0
$u
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=30425876
$z
click for full text (PQDT)
筆 0 讀者評論
館藏地:
全部
電子資源
出版年:
卷號:
館藏
1 筆 • 頁數 1 •
1
條碼號
典藏地名稱
館藏流通類別
資料類型
索書號
使用類型
借閱狀態
預約狀態
備註欄
附件
W9485880
電子資源
11.線上閱覽_V
電子書
EB
一般使用(Normal)
在架
0
1 筆 • 頁數 1 •
1
多媒體
評論
新增評論
分享你的心得
Export
取書館
處理中
...
變更密碼
登入