Ultraviolet Photodissociation Mass Spectrometry for Analysis of Biological Molecules

Characterization of hydrogen bonding motifs in proteins: hydrogen elimination monitoring by ultraviolet photodissociation mass spectrometry.

Determination of structure and folding of certain classes of proteins remains intractable by conventional structural characterization strategies and has spurred the development of alternative methodologies. Mass spectrometry-based approaches have a unique capacity to differentiate protein heterogeneity due to the ability to discriminate populations, whether minor or major, featuring modificatio...

Frontiers in Mass Spectrometry for Analysis of Biological Molecules – Proteomics, Metabolomics and Imaging

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Structural characterization of holo- and apo-myoglobin in the gas phase by ultraviolet photodissociation mass spectrometry.

Ultraviolet photodissociation (UVPD) mass spectrometry is employed to investigate the structure of holo-myoglobin as well as its apo form transferred to the gas phase by native electrospray. UVPD provided insight into the stability of native structural elements of holo-myoglobin. The fragmentation yields from UVPD showed the greatest overall correlation with B-factors generated from the crystal...

Charge site assignment in native proteins by ultraviolet photodissociation (UVPD) mass spectrometry.

Characterization of all gas-phase charge sites of natively sprayed proteins and peptides is demonstrated using 193 nm UVPD. The high sequence coverage offered by UVPD is exploited for the accurate determination of charge sites in protein systems up to 18 kDa, allowing charge site to be studied as a function of protein conformation and the presence of disulfide bonds. Charging protons are found ...

Analysis of Biological Molecules on Surfaces Using Stimulated Desorption Photoionization Mass Spectrometry