Enhanced Declustering Enables Native Top-Down Analysis of Membrane Protein Complexes using Ion-Mobility Time-Aligned Fragmentation.

Native mass spectrometry (MS) is proving to be a disruptive technique for studying the interactions of proteins, necessary for understanding the functional roles of these biomolecules. Recent research is expanding the application of native MS towards membrane proteins directly from isolated membrane preparations or from purified detergent micelles. The former results in complex spectra comprising several heterogeneous protein complexes; the latter enables therapeutic protein targets to be screened against multiplexed preparations of compound libraries.

A global database to catalogue the impacts of agricultural management practices on terrestrial biodiversity.

Habitat loss and degradation due to global agriculture land use is a major threat to biodiversity. Identifying agricultural management practices that mitigate these impacts is urgently needed. Thousands of experiments have been conducted worldwide in the last decades to compare the impacts of various agricultural management practices on biodiversity.

Existing evidence on the impact of changes in marine ecosystem structure and functioning on ecosystem service delivery: a systematic map.

Background: The current biodiversity crisis underscores the urgent need for sustainable management of the human uses of nature. In the context of sustainability management, adopting the ecosystem service (ES) concept, i.e.

Full Separation and Sequencing of Isomeric Proteoforms in the Middle-Down Mass Range Using Cyclic Ion Mobility and Electron Capture Dissociation.

Unambiguous identification of distinct proteoforms and their biological functions is a significant analytical challenge due to the many combinations of post-translational modifications (PTM) that generate isomeric proteoforms. Resulting chimeric tandem mass spectra hinder detailed structural characterization of individual proteoforms for mixtures with more than two isomers. Large isomeric peptides and intact isomeric proteins are extremely difficult to distinguish with traditional chromatographic separation methods.