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- W4256028375 abstract "This chapter provides a description of two different studies, one of DNA-binding proteins and the other using the interactomic technology of phage display, which have, inadvertently, provided some evidence of the commonality of protein moonlighting in eukaryotes and prokaryotes. A potentially more attractive set of methodologies to identify large numbers of moonlighting proteins are the various techniques which come under the heading of protein interactomics. Mass spectrometry-based proteomics can be used for this purpose, but other methods, to be described, can handle larger populations of interacting ligands. The prevailing hypothesis concerning the evolution of protein function is that most mutations do not influence the biological function/activity of proteins and so they are termed neutral. The function of proteins depends on their amino acid sequences and the associated three-dimensional structures these sequences allow to be generated. Mutations in genes can give rise to alterations in individual amino acids or alterations of larger segments of the sequence." @default.
- W4256028375 created "2022-05-12" @default.
- W4256028375 date "2016-12-14" @default.
- W4256028375 modified "2023-10-17" @default.
- W4256028375 title "Protein Moonlighting" @default.
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- W4256028375 doi "https://doi.org/10.1002/9781118952108.ch9" @default.
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