Abstract
Genomic sequences are becoming available with increasing speed as a result of the advances in gene technology. Nevertheless, both covalent and noncovalent modifications can occur in the corresponding protein sequence before the protein is fully functional, so it is important to know the actual protein sequence to understand its function [1, 2]. It is equally important to determine the higher order protein structure, and its interaction with other biological components. Noncovalent interactions of this type play a key role in molecular recognition phenomena such as enzyme-substrate interaction, receptor-ligand binding, formation of oligomeric proteins, assembly of transcription factors, and formation of cellular structures themselves [3–4].
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Krutchinsky, A.N., Chernushevich, I.V., Loboda, A.V., Ens, W., Standing, K.G. (2000). Measurements of Protein Structure and Noncovalent Interactions by Time-of-Flight Mass Spectrometry with Orthogonal Ion Injection. In: Burlingame, A.L., Carr, S.A., Baldwin, M.A. (eds) Mass Spectrometry in Biology & Medicine. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-59259-719-2_2
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DOI: https://doi.org/10.1007/978-1-59259-719-2_2
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