자료유형  

 학위논문

Control Number  

0017164607

International Standard Book Number  

9798346745044

Dewey Decimal Classification Number  

543

Main Entry-Personal Name  

Sharon, Edith.

Publication, Distribution, etc. (Imprint  

[S.l.] : Indiana University., 2024

Publication, Distribution, etc. (Imprint  

Ann Arbor : ProQuest Dissertations & Theses, 2024

Physical Description  

290 p.

General Note  

Source: Dissertations Abstracts International, Volume: 86-06, Section: B.

General Note  

Advisor: Clemmer, David E.

Dissertation Note  

Thesis (Ph.D.)--Indiana University, 2024.

Summary, Etc.  

요약Molecular structure is traditionally determined by techniques such as crystallography, microscopy, and NMR. However, species such as non-native protein structures can be difficult to characterize with these approaches due to their transience and low-abundance. Ion mobility spectrometry mass spectrometry, while lacking atomic resolution, provides another means of measuring structure. In this work, we leverage cyclic ion mobility spectrometry to increase the path length and perform tandem ion mobility separations. This technique is used to characterize diastereomer content in therapeutic oligonucleotides containing phosphorothioate linkages and is demonstrated to effectively separate diastereomers in fragments from these species. It is also applied to hemoglobin to demonstrate the capability of the technique for further understanding the variety of conformations that encompass the structural landscape of this protein. These structures are later examined for their relationship to hemoglobin's oxygen binding capabilities and the conformational changes associated with this binding activity. This work provides additional evidence for the hypothesis that many structures are involved in these changes beyond the two that were determined in original crystallography studies. Finally, we apply this technique to a larger system, the rat 20S proteasome. We find evidence for similarities between the thermal stabilities of the proteasome and the immunoproteasome as well as evidence for a structural change that was not detected in previous studies of the yeast proteasome. Collectively, this work demonstrates the power of cyclic ion mobility for characterization of structural aspects of biomolecules.

Subject Added Entry-Topical Term  

Analytical chemistry.

Subject Added Entry-Topical Term  

Chemistry.

Subject Added Entry-Topical Term  

Molecular chemistry.

Index Term-Uncontrolled  

Cyclic ion mobility

Index Term-Uncontrolled  

Ion mobility

Index Term-Uncontrolled  

Mas spectrometry

Index Term-Uncontrolled  

Oligonucleotides

Index Term-Uncontrolled  

Crystallography

Added Entry-Corporate Name  

Indiana University Chemistry

Host Item Entry  

Dissertations Abstracts International. 86-06B.

Electronic Location and Access  

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Control Number  

joongbu:656576