Loops Linking Secondary Structure Elements Affect the Stability of the Molten Globule Intermediate State of Apomyoglobin
Document Type
Article
Publication Date
2020
Keywords
apomyoglobin, chevron plot, energy profile, molten globule, protein folding, tryptophan fluorescence
Digital Object Identifier (DOI)
https://doi.org/10.1002/1873-3468.13905
Abstract
Apomyoglobin is a widely used model for studying the molecular mechanisms of globular protein folding. This work aimed to analyze the effects of rigidity and length of loops linking protein secondary structure elements on the stability of the molten globule intermediate state. For this purpose, we studied folding/unfolding of mutant apomyoglobin forms with substitutions of loop-located proline residues to glycine and with loop extension by three or six glycine residues. The kinetic and equilibrium experiments performed gave an opportunity to calculate free energies of different apomyoglobin states. Our analysis revealed that the mutations introduced into the apomyoglobin loops have a noticeable effect on the stability of the intermediate state compared to the unfolded state.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
FEBS Letters, v. 594, issue 20, p. 3293-3304
Scholar Commons Citation
Majorina, Maria A.; Balobanov, Vitaly A.; Uversky, Vladimir N.; and Melnik, Bogdan S., "Loops Linking Secondary Structure Elements Affect the Stability of the Molten Globule Intermediate State of Apomyoglobin" (2020). Molecular Medicine Faculty Publications. 184.
https://digitalcommons.usf.edu/mme_facpub/184
