Sgobba, Elvira
- Department of Forest Genetics and Plant Physiology, Swedish University of Agricultural Sciences
Abstract
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.
Keywords
MALDI; protein assembly; noncovalent interactions
Published in
Molecules (Basel, Switzerland)
2020, volume: 25, number: 21, article number: 4979
Publisher: MDPI
SLU Authors
UKÄ Subject classification
Biochemistry
Molecular Biology
Publication identifier
- DOI: https://doi.org/10.3390/molecules25214979
Permanent link to this page (URI)
https://res.slu.se/id/publ/109362