The function of the conserved “non-functional” residues in apomyoglobin is to provide and preserve the correct protein topology

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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.

Sobre autores

V. Bychkova

Institute of Protein Research, Russian Academy of Sciences

142290 Pushchino, Moscow Region, Russia

D. Dolgikh

Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences

117871 Moscow, Russia

V. Balobanov

Institute of Protein Research, Russian Academy of Sciences

Email: balobanov@phys.protres.ru
142290 Pushchino, Moscow Region, Russia

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