MINI-REVIEW: Function of the Conserved Non-Functional Residues in Apomyoglobin – to Determine and to Preserve Correct Topology of the Protein

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Valentina E. Bychkova¹, Dmitry A. Dolgikh², and Vitalii A. Balobanov^1,a*

¹Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia

²Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117871 Moscow, Russia

^* To whom correspondence should be addressed.

Received July 18, 2023; Revised July 18, 2023; Accepted August 31, 2023

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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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KEY WORDS: apomyoglobin, conserved residues, protein stability, protein folding, native topology

DOI: 10.1134/S0006297923110184

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