Using electrospray ionisation mass spectrometry to study non-covalent interactions.
The key strengths of electrospray over any other ionisation techniques are its soft nature and its ability to produce multiply charged ions. This combination is ideal for the study of non-covalent interactions. In this review article, we cover the basics of studying non-covalent interactions by mass spectrometry--illustrated with examples from our own and other labs--and discuss the current mass spectrometry based methods used for understanding and characterising non-covalent protein complexes.
McCullough
Bryan J
BJ
The Michael Barber Centre for Mass Spectrometry, The University of Manchester, Manchester Interdisciplinary Biocentre, The John Garside Building, 131 Princess Street, Manchester M17DN, UK.
Gaskell
Simon J
SJ
D005740:Gases / Q000737:chemistry; D007553:Isotope Labeling; D008024:Ligands; D011485:Protein Binding; D011489:Protein Denaturation; D011506:Proteins / Q000032:analysis / Q000737:chemistry / Q000378:metabolism*; D012997:Solvents / Q000737:chemistry; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods*; D053719:Tandem Mass Spectrometry / Q000379:methods
D005740:Gases; D008024:Ligands; D011506:Proteins; D012997:Solvents