Sgobba, Elvira
- Institutionen för skoglig genetik och växtfysiologi, Sveriges lantbruksuniversitet
Översiktsartikel2020Vetenskapligt granskadÖppen tillgång
Giampa, Marco; Sgobba, Elvira
Noncovalent interactions are the keys to the structural organization of biomolecule e.g., proteins, glycans, lipids in the process of molecular recognition processes e.g., enzyme-substrate, antigen-antibody. Protein interactions lead to conformational changes, which dictate the functionality of that protein-protein complex. Besides biophysics techniques, noncovalent interaction and conformational dynamics, can be studied via mass spectrometry (MS), which represents a powerful tool, due to its low sample consumption, high sensitivity, and label-free sample. In this review, the focus will be placed on Matrix-Assisted Laser Desorption Ionization Mass Spectrometry (MALDI-MS) and its role in the analysis of protein-protein noncovalent assemblies exploring the relationship within noncovalent interaction, conformation, and biological function.
MALDI; protein assembly; noncovalent interactions
Molecules (Basel, Switzerland)
2020, Volym: 25, nummer: 21, artikelnummer: 4979
Utgivare: MDPI
Biokemi och molekylärbiologi
DOI: https://doi.org/10.3390/molecules25214979
https://res.slu.se/id/publ/109362