AI Article Synopsis
- Development of chemical chaperones has improved the analysis of membrane protein complexes in water, allowing for better stability and interaction studies.
- Ultraviolet photodissociation (UVPD) technique enhances protein sequence analysis, offering more detailed insights into proteins like ammonia channel (AmtB) and aquaporin Z (AqpZ).
- Initial findings suggest changes in UVPD sequences can indicate structural shifts in the mechanosensitive channel of large conductance (MscL) when interacting with different phospholipids.
Article Abstract
Development of chemical chaperones to solubilize membrane protein complexes in aqueous solutions has allowed for gas-phase analysis of their native-like assemblies, including rapid evaluation of stability and interacting partners. Characterization of protein primary sequence, however, has thus far been limited. Ultraviolet photodissociation (UVPD) generates a multitude of sequence ions for the ammonia channel (AmtB), provides improved localization of a possible post-translational modification of aquaporin Z (AqpZ), and surpasses previous reports of sequence coverage for mechanosensitive channel of large conductance (MscL). Variations in UVPD sequence ion abundance have been shown to correspond to structural changes induced upon some perturbation. Preliminary results are reported here for elucidating increased rigidity or flexibility of MscL when bound to various phospholipids.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6949371 | PMC |
| http://dx.doi.org/10.1021/acs.analchem.9b03689 | DOI Listing |
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