The Electrospray Ionization (ESI) is a soft ionization technique extensively used for production of gas phase ions (without fragmentation) of thermally labile large supramolecules. In the present review we have described the development of Electrospray Ionization mass spectrometry (ESI-MS) during the last 25 years in the study of various properties of different types of biological molecules. There have been extensive studies on the mechanism of formation of charged gaseous species by the ESI. Several groups have investigated the origin and implications of the multiple charge states of proteins observed in the ESI-mass spectra of the proteins. The charged analytes produced by ESI can be fragmented by activating them in the gas-phase, and thus tandem mass spectrometry has been developed, which provides very important insights on the structural properties of the molecule. The review will highlight recent developments and emerging directions in this fascinating area of research. 1. Introduction The basic concepts of chemistry originated from the quantitative estimation (e.g., weighing) of the constituents in a chemical reaction during the period of Lavoisier more than 200 years ago. Since then the analytical measurement of masses of the samples continuously evolved through the gravimetric analysis to weighing a single atom/molecule using the modern instrument called mass spectrometer. In mass spectrometry, a particular state of matter called gaseous ionic state is studied by transferring the analytes from condensed phase to the gas phase followed by their ionization. The success of the study of gas-phase ion chemistry and its application has been driven by the continuous advancement of the mass spectrometric technique since the studies were performed by Thomson [1]. As a result the mass spectrometry has become one of the most sensitive analytical methods for the structural characterization of molecules. Before the development of ESI-MS, there were several ionization methods (electron ionization, chemical ionization, etc.), but none of them could be able to overcome the propensity of the analyte fragmentation. In the mid 1980s, it became indispensable to precisely measure the molecular mass of the biologically important supramolecules like proteins [2]. But the proteins are polar, nonvolatile, and thermally labile molecules. So the ionization of the proteins by conventional ionization methods could lead to structural destruction. Although a technique called fast atom bombardment (FAB) [3] was available that time for the ionization of the biological samples,
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