2020
DOI: 10.3390/molecules25214979
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Insight to Functional Conformation and Noncovalent Interactions of Protein-Protein Assembly Using MALDI Mass Spectrometry

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 consum… Show more

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Cited by 11 publications
(3 citation statements)
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References 142 publications
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“…Although most tandem mass spectrometry-based proteomic studies in biomedical research use ESI as an ionization source [ 60 ], MALDI-ToF/ToF tandem mass spectrometry remains a relatively simple and fast alternative to perform qualitative and quantitative analysis of amino and organic acids [ 6 ], proteins and peptides [ 61 ], protein–protein interactions (PPIs), and post-translational modifications (PTMs). A variety of peptides and proteins become biomarkers for clinical applications due to useful features, such as user-friendly sample preparation [ 62 ], preservation of non-covalent interactions, and high sensitivity, high-throughput screening procedures/fast data acquisition [ 63 ].…”
Section: Applications Of Maldi-ms/ms-based Proteomicsmentioning
confidence: 99%
“…Although most tandem mass spectrometry-based proteomic studies in biomedical research use ESI as an ionization source [ 60 ], MALDI-ToF/ToF tandem mass spectrometry remains a relatively simple and fast alternative to perform qualitative and quantitative analysis of amino and organic acids [ 6 ], proteins and peptides [ 61 ], protein–protein interactions (PPIs), and post-translational modifications (PTMs). A variety of peptides and proteins become biomarkers for clinical applications due to useful features, such as user-friendly sample preparation [ 62 ], preservation of non-covalent interactions, and high sensitivity, high-throughput screening procedures/fast data acquisition [ 63 ].…”
Section: Applications Of Maldi-ms/ms-based Proteomicsmentioning
confidence: 99%
“…39 MALDI MS was also used for studying molecular interactions at micro and macromolecular levels. 18,40,41 Furthermore, this technique is also used to study drug or nanoparticlemicrobe interactions 18 in which the molecular proles obtained from the bacteria aer nanoparticle treatment have been used for identifying the mode of interaction of nanoparticles with bacterial cells. However, these studies did not focus on one of the most signicant molecules in bacteria, namely lipids, on which nanoparticles act during interactions.…”
Section: Introductionmentioning
confidence: 99%
“…Different from typical covalent bonds with shared electron pairs between interacting atoms formed mainly by the occupied orbital overlapping, which serve as fundamental building blocks to build molecules and determine the properties to a large extent, noncovalent interactions [1][2][3] exist at a longer range and have weaker strength. These noncovalent interactions have drawn considerable attention in various fields related to chemistry such as catalytic synthesis, 4,5 advanced functional materials, [6][7][8] crystal engineering, [9][10][11][12] biological macromolecules, [13][14][15] and molecular recognition 16,17 due to nonnegligible effects during the formation of molecular clusters in objective systems.…”
Section: Introductionmentioning
confidence: 99%