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Loops linking secondary structure elements affect the stability of the molten globule intermediate state of apomyoglobin
Author(s) -
Majorina Maria A.,
Balobanov Vitaly A.,
Uversky Vladimir N,
Melnik Bogdan S.
Publication year - 2020
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13905
Subject(s) - molten globule , chemistry , protein folding , folding (dsp implementation) , folding funnel , intermediate state , protein secondary structure , crystallography , native state , equilibrium unfolding , phi value analysis , globular protein , contact order , downhill folding , biophysics , biochemistry , biology , physics , atomic physics , electrical engineering , engineering
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.