Molten Globular Enzymes
Document Type
Book Chapter
Publication Date
2023
Keywords
Protein Folding, Partially Folded Folding Intermediate, Molten Globule, Designed Protein, Circular Permutation
Digital Object Identifier (DOI)
https://doi.org/10.1016/B978-0-323-99533-7.00010-8
Abstract
Structural biology of enzymatic catalysis posits that structure defines function. This idea is deeply rooted in the “lock-and-key” perspective of the enzyme action. Although some flexibility is accepted in the form of “induced fit” or “conformational selection,” these models do not expect excessive conformational diversity of a protein molecule. In other words, since facilitation of the formation of the transition state of the chemical reaction to be catalyzed depends on a well-organized environment in the active site of the enzyme, enzymatic catalysis is poorly compatible with structural disorder. However, there is growing evidence of the existence of catalytic disordered proteins. Furthermore, since the chance of the spontaneous emergence of a fully folded protein with fully defined catalytic function is negligible, disordered proteins acted as precursors of the modern-day enzymes. This chapter represents an overview of the molten globular enzymes and represents several illustrative examples of this important phenomenon.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Molten Globular Enzymes, in M. N. Gupta & V. N. Uversky (Eds.), Structure and Intrinsic Disorder in Enzymology, Academic Press, p. 303-325
Scholar Commons Citation
Uversky, Vladimir N., "Molten Globular Enzymes" (2023). Molecular Medicine Faculty Publications. 1117.
https://digitalcommons.usf.edu/mme_facpub/1117
