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Developing Ion Mobility Spectrometry...

Conant, Chris Robin.

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Developing Ion Mobility Spectrometry-Mass Spectrometry Techniques to Study the Effects of Proline on Peptide Structure in Solution and in the Gas Phase.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Developing Ion Mobility Spectrometry-Mass Spectrometry Techniques to Study the Effects of Proline on Peptide Structure in Solution and in the Gas Phase./
作者:	Conant, Chris Robin.
出版者:	Ann Arbor : ProQuest Dissertations & Theses, : 2019,
面頁冊數:	202 p.
附註:	Source: Dissertations Abstracts International, Volume: 80-09, Section: B.
Contained By:	Dissertations Abstracts International80-09B.
標題:	Chemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=13428541
ISBN:	9780438886476

Developing Ion Mobility Spectrometry-Mass Spectrometry Techniques to Study the Effects of Proline on Peptide Structure in Solution and in the Gas Phase.
Conant, Chris Robin.

Developing Ion Mobility Spectrometry-Mass Spectrometry Techniques to Study the Effects of Proline on Peptide Structure in Solution and in the Gas Phase. - Ann Arbor : ProQuest Dissertations & Theses, 2019 - 202 p.

Source: Dissertations Abstracts International, Volume: 80-09, Section: B.

Thesis (Ph.D.)--Indiana University, 2019.

This item must not be added to any third party search indexes.

IMS-MS is a well-developed technique for the study of biomolecular structure. Here, we investigate the effects of proline on peptide conformation. Proline is unique among the 20 common amino acids as it forms both cis and trans isomers. Proline isomerization has important biological ramifications as it is frequently the rate limiting step of protein folding and can induce large structural changes in peptides. The first study here focuses on the neuropeptide substance P (subP) with the sequence Arg 1-Pro2-Lys3-Pro4-Gln 5-Gln6-Phe7-Phe8-Glu 9-Leu10-Met11-NH2, which undergoes spontaneous degradation when heated in solution. This reaction mechanism involves protonation of [subP+2H]2+→[subP+3H]3+ preceding cleavage of the Pro2-Lys3 bond to form cyclo(Arg1-Pro2), followed by cleavage of the Pro4-Gln5 bond to form cyclo(Lys 3-Pro4). These processes likely involve trans→cis isomerization of Arg1-Pro2 and Lys 3-Pro4 bonds, respectively. The second study characterizes four mobility peaks observed for [subP+3H]3+. Mobility-selection and collisional activation indicates that the three most compact peaks correspond to kinetically trapped solution structures with the final peak representing the extended gas-phase structure. Additionally, there is evidence for a fourth kinetically trapped solution structure unresolved from the peak corresponding to the gas-phase structure. The third study explores the gas-phase fragmentation pathways of subP for a comparison with the solution-phase dissociation process. The final study investigates the effects of phosphorylation on a library of tumor-specific phosphopeptides associated with the major histocompatibility complex. These peptides possess N-terminal Xaa1-Pro 2 motifs and phosphoserine at the fourth amino acid. Incubation of these peptides at elevated solution temperatures finds that dissociation of Xaa1-Pro2 occurs generally among these peptides and this dissociation acts as a measure of stability. Phosphorylation correlates with decreased dissociation rates, suggesting strong interactions between the phosphate group and the N-terminal amine that restrict the ability of many of these peptides to undergo cis/trans-isomerization, preventing bond cleavage. The results presented here demonstrate the utility of using IMS-MS to monitor changes in solution- and gas-phase structures to gain insight into peptide structure and stability.

ISBN: 9780438886476Subjects--Topical Terms:

516420
Chemistry.

Developing Ion Mobility Spectrometry-Mass Spectrometry Techniques to Study the Effects of Proline on Peptide Structure in Solution and in the Gas Phase.
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520 $a IMS-MS is a well-developed technique for the study of biomolecular structure. Here, we investigate the effects of proline on peptide conformation. Proline is unique among the 20 common amino acids as it forms both cis and trans isomers. Proline isomerization has important biological ramifications as it is frequently the rate limiting step of protein folding and can induce large structural changes in peptides. The first study here focuses on the neuropeptide substance P (subP) with the sequence Arg 1-Pro2-Lys3-Pro4-Gln 5-Gln6-Phe7-Phe8-Glu 9-Leu10-Met11-NH2, which undergoes spontaneous degradation when heated in solution. This reaction mechanism involves protonation of [subP+2H]2+→[subP+3H]3+ preceding cleavage of the Pro2-Lys3 bond to form cyclo(Arg1-Pro2), followed by cleavage of the Pro4-Gln5 bond to form cyclo(Lys 3-Pro4). These processes likely involve trans→cis isomerization of Arg1-Pro2 and Lys 3-Pro4 bonds, respectively. The second study characterizes four mobility peaks observed for [subP+3H]3+. Mobility-selection and collisional activation indicates that the three most compact peaks correspond to kinetically trapped solution structures with the final peak representing the extended gas-phase structure. Additionally, there is evidence for a fourth kinetically trapped solution structure unresolved from the peak corresponding to the gas-phase structure. The third study explores the gas-phase fragmentation pathways of subP for a comparison with the solution-phase dissociation process. The final study investigates the effects of phosphorylation on a library of tumor-specific phosphopeptides associated with the major histocompatibility complex. These peptides possess N-terminal Xaa1-Pro 2 motifs and phosphoserine at the fourth amino acid. Incubation of these peptides at elevated solution temperatures finds that dissociation of Xaa1-Pro2 occurs generally among these peptides and this dissociation acts as a measure of stability. Phosphorylation correlates with decreased dissociation rates, suggesting strong interactions between the phosphate group and the N-terminal amine that restrict the ability of many of these peptides to undergo cis/trans-isomerization, preventing bond cleavage. The results presented here demonstrate the utility of using IMS-MS to monitor changes in solution- and gas-phase structures to gain insight into peptide structure and stability.
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