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Development of MS-based Methodologie...
~
Loziuk, Philip Lawrence.
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Development of MS-based Methodologies for Discovery, Quantitative Proteomics, Post-Translational Modification Profiling and TransOMIC Pathway Approaches in Complex Biological Systems.
紀錄類型:
書目-電子資源 : Monograph/item
正題名/作者:
Development of MS-based Methodologies for Discovery, Quantitative Proteomics, Post-Translational Modification Profiling and TransOMIC Pathway Approaches in Complex Biological Systems./
作者:
Loziuk, Philip Lawrence.
出版者:
Ann Arbor : ProQuest Dissertations & Theses, : 2016,
面頁冊數:
409 p.
附註:
Source: Dissertation Abstracts International, Volume: 78-08(E), Section: B.
Contained By:
Dissertation Abstracts International78-08B(E).
標題:
Analytical chemistry. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10585389
ISBN:
9781369638615
Development of MS-based Methodologies for Discovery, Quantitative Proteomics, Post-Translational Modification Profiling and TransOMIC Pathway Approaches in Complex Biological Systems.
Loziuk, Philip Lawrence.
Development of MS-based Methodologies for Discovery, Quantitative Proteomics, Post-Translational Modification Profiling and TransOMIC Pathway Approaches in Complex Biological Systems.
- Ann Arbor : ProQuest Dissertations & Theses, 2016 - 409 p.
Source: Dissertation Abstracts International, Volume: 78-08(E), Section: B.
Thesis (Ph.D.)--North Carolina State University, 2016.
Aided by the increasingly greater amounts of qualitative and quantitative information that can be obtained from a systems biology approach, the new age of OMICs data has demonstrated the ability to solve complex biological problems. The field of mass spectrometry based proteomics and metabolomics has provided many solutions to the intricate biochemistry posed by biology. From sample preparation to instrumentation, from the fundamentals to applications, these areas have been driven by the necessity to provide speed, sensitivity, specificity and high-thoughput, quantitative chemical information. The work described here focuses on utilizing new technology to develop mass spectrometry based workflows for quantitatively characterizing proteins and metabolites in the monolignol and cellulose/hemicellulose biosynthetic pathway.
ISBN: 9781369638615Subjects--Topical Terms:
3168300
Analytical chemistry.
Development of MS-based Methodologies for Discovery, Quantitative Proteomics, Post-Translational Modification Profiling and TransOMIC Pathway Approaches in Complex Biological Systems.
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Aided by the increasingly greater amounts of qualitative and quantitative information that can be obtained from a systems biology approach, the new age of OMICs data has demonstrated the ability to solve complex biological problems. The field of mass spectrometry based proteomics and metabolomics has provided many solutions to the intricate biochemistry posed by biology. From sample preparation to instrumentation, from the fundamentals to applications, these areas have been driven by the necessity to provide speed, sensitivity, specificity and high-thoughput, quantitative chemical information. The work described here focuses on utilizing new technology to develop mass spectrometry based workflows for quantitatively characterizing proteins and metabolites in the monolignol and cellulose/hemicellulose biosynthetic pathway.
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Initially, the quantitative assay for monolignol enzymes was used as a controlled system study for previous findings of peptide decay. By use of design of experiments, the major source of peptide decay was attributed largely to the non-specific activity of trypsin. This had major implications across the proteomics community as it fundamentally impacted the limit of detection and precision of virtually all MS-based quantitative measurements. Further utilizing the monolignol pathway as a model system, a new approach was developed to systematically assess fragment ion purity which is a critical aspect of MS/MS quantification of proteins. The variability of conserved ion dissociation was discovered to be dynamic, contrary to what was previously accepted by the field of proteomics. This inherent experimental variability was used to establish thresholds and successfully improve the processing of large quantitative data sets.
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The development and understanding of these fundamental steps in MS-based proteomic workflows led to further biological insights as they were applied to the systems study of lignin and cellulose/hemicellulose biosynthesis. In applying this knowledge, transcription factors regulating lignocellulose biosynthesis were characterized at the protein level for the first time. These findings were further utilized to develop a quantitative assay for 14 enzymes involved in cellulose biosynthesis. This represented the first quantitative measurements for proteins involved in cellulose biosynthesis.
520
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Novel MS-based approaches were also developed for studying post translational modifications and gain further insight into mechanisms regulating lignin biosynthesis. Phosphopeptide enrichment strategies were implemented to profile the phopshoproteome of the model woody plant Populus trichocarpa. Previously uncharacterized phosphorylation events were localized to proteins in the monolignol biosynthetic pathway. The monolignol protein OMT2 was used to develop an in vitro assay for inducing phosphorylation by native molecular machinery. Targeted MS based methods were then developed to identify and quantitatively assess the occupancy of phosphorylation. This information could then be correlated with a reduction in enzymatic activity. For the first time a specific phosphorylation event was found to be an on/off switch for monolignol biosynthesis. These methods have the potential to be applied to other systems and the findings had a major impact on our model and fundamental understanding of lignin biosynthetic flux. Finally, another biologically significant post translational modification, glycosylation, is explored. This area of proteomics has been understudied due to the complex nature of glycans and glycoproteins. Newly developed technology from our research group was implemented to elucidate glycosylation sites and glycans within the P. trichocarpa proteome and more specifically, the monolignol pathway. Many of these represent the first insights into glycosylation and its possible role in regulating lignin biosynthesis. These findings present a foundation of knowledge which will provide the ability to advance our depth of understanding of lignocellulose biosynthesis, plant proteomics and the field of mass spectrometry.
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