Formation of the Native Topology of a Protein is due to the "Conserved but Non-Functional" Residues: A Case of Apomyoglobin Folding

This paper is dedicated to the memory of Oleg B. Ptitsyn (1929-1999) and presents an answer to his question: "What is the role of conserved non-functional residues in protein folding?". This answer follows from the experimental works of three labs. The role of non-functional but conserved...

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Bibliographic Details
Published in:Frontiers in bioscience (Landmark. Print) 2024-11, Vol.29 (11), p.379
Main Authors: Bychkova, Valentina E, Dolgikh, Dmitry A, Balobanov, Vitalii A, Finkelstein, Alexei V
Format: Article
Language:English
Subjects:
Animals
apomyoglobin
Apoproteins - chemistry
Apoproteins - genetics
Apoproteins - metabolism
conserved residues
Conserved Sequence
folding intermediate
globin
Models, Molecular
Myoglobin - chemistry
Myoglobin - metabolism
native fold topology
non-functional residues
Protein Folding
protein stability
Protein Structure, Secondary
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Summary:This paper is dedicated to the memory of Oleg B. Ptitsyn (1929-1999) and presents an answer to his question: "What is the role of conserved non-functional residues in protein folding?". This answer follows from the experimental works of three labs. The role of non-functional but conserved residues of apomyoglobin (apoMb) in the formation of the native protein fold in the molten globule state has been experimentally revealed. This research proves that the non-functional but conserved residues of apoMb are necessary for the formation and maintenance of the correct topological arrangement of the main elements in the apoMb secondary structure already in the early folding intermediate.
ISSN:2768-6698
2768-6701
2768-6698
DOI:10.31083/j.fbl2911379