Abstract
In this paper the answer to O. B. Ptitsyn’s question “What is the role of conserved non-functional residues in apomyoglobin” is presented, which is based on the research results of three laboratories. The role of conserved non-functional apomyoglobin residues in formation of native topology in the molten globule state of this protein is revealed. This fact allows suggesting that the conserved non-functional residues in this protein are indispensable for fixation and maintaining main elements of the correct topology of its secondary structure in the intermediate state. The correct topology is a native element in the intermediate state of the protein.
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Notes
P. Wright, The Scripss Research Institute, La Jolla, CA 92037, USA.
H. Roder, Fox Chase Cancer Center, 333 Cottman Ave, Philadelphia, PA 19111.
Abbreviations
- A, G and H:
-
main alpha-helices of apoMb
- L:
-
an intermediate state in the folding of apoMb
- MG:
-
molten globule state
- N and U:
-
native and unfolded states of protein
- SW apoMb:
-
wild type of sperm-whale apomyoglobin
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Acknowledgments
Authors express their gratitude to P.E. Wright for his help, support and structural data, H. Roder and his collaborators for excellent experiments and valuable discussions, to A. V. Finkelstein for valuable remarks, E. V. Serebrova for help in preparing the manuscript, and all collaborators participated in the study of apomyoglobin.
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V.E.B. and D.A.D carried out additional analysis of the experimental data; V.E.B., D.A.D., and V.A.B. participated in the paper writing.
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The authors declare no conflict of interest in financial or any other sphere. This article does not contain any studies with human participants or animals performed by any of the authors.
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Dedicated to memory of Oleg B. Ptitsyn
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Bychkova, V.E., Dolgikh, D.A. & Balobanov, V.A. Function of the Conserved Non-Functional Residues in Apomyoglobin – to Determine and to Preserve Correct Topology of the Protein. Biochemistry Moscow 88, 1905–1909 (2023). https://doi.org/10.1134/S0006297923110184
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DOI: https://doi.org/10.1134/S0006297923110184