Sgobba, Elvira
- Institutionen för skoglig genetik och växtfysiologi, Sveriges lantbruksuniversitet
Sammanfattning
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.
Nyckelord
MALDI; protein assembly; noncovalent interactions
Publicerad i
Molecules (Basel, Switzerland)
2020, volym: 25, nummer: 21, artikelnummer: 4979
Utgivare: MDPI
SLU författare
UKÄ forskningsämne
Biokemi
Molekylärbiologi
Publikationens identifierare
- DOI: https://doi.org/10.3390/molecules25214979
Permanent länk till denna sida (URI)
https://res.slu.se/id/publ/109362