Proteomics

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Characterization of disulfide linkages in proteins by 193 nm ultraviolet photodissociation (UVPD)

ABSTRACT: Inter-linked disulfide bonds connecting peptide chains are homolytically cleaved with 193 nm ultraviolet photodissociation (UVPD). Analysis of insulin demonstrates the ability for UVPD to cleave multiple disulfide bonds and provide sequence coverage of multiple peptide chains in the same MS/MS event. The information provided by UVPD of disulfide-bound peptides is comparable to information garnered from other high energy dissociation methods but requires an activation period an order of magnitude faster than these methods. This phenomenon was investigated, along with a partial reduction and alkylation sample preparation to determine disulfide connectivities of enzymatically digested proteins. The 4 disulfide bonds of lysozyme and the 19 disulfide bonds of serotransferrin were unambiguously characterized through non-reduced and partially reduced protein digestions. 

ORGANISM(S): Homo Sapiens (human) Gallus Gallus Bos Taurus

SUBMITTER: Jennifer S. Brodbelt 

PROVIDER: PXD009460 | JPOST Repository | Sat Apr 28 00:00:00 BST 2018

REPOSITORIES: jPOST

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Dataset's files

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Action DRS
EThcD%20Insulin.raw Raw
Lysozyme_2p2mJ_10minute.raw Raw
Lysozyme_2p2mJ_1minute.raw Raw
Lysozyme_2p2mJ_20minute.raw Raw
Lysozyme_2p2mJ_30minute.raw Raw
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Characterization of Disulfide Linkages in Proteins by 193 nm Ultraviolet Photodissociation (UVPD) Mass Spectrometry.

Quick M Montana MM   Crittenden Christopher M CM   Rosenberg Jake A JA   Brodbelt Jennifer S JS  

Analytical chemistry 20180628 14

Deciphering disulfide bond patterns in proteins remains a significant challenge. In the present study, interlinked disulfide bonds connecting peptide chains are homolytically cleaved with 193 nm ultraviolet photodissociation (UVPD). Analysis of insulin showcased the ability of UVPD to cleave multiple disulfide bonds and provide sequence coverage of the peptide chains in the same MS/MS event. For proteins containing more complex disulfide bonding patterns, an approach combining partial reduction  ...[more]

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