Intermediate states of apomyoglobin: Are they parts of the same area of conformations diagram?

Balobanov, Vitaly A.; Katina, N. S.; Finkelstein, Alan; Bychkova, Valentina E.

doi:10.1134/s0006297917050108

Cited by 6 publications

(5 citation statements)

References 27 publications

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“…The holo form of this protein, containing the heme cofactor, occupies a special place in chemistry and biology as it was the very first protein whose structure was solved by X-ray crystallography. In addition, apoMb carries the ubiquitous all-α-helical globin fold. , and its in vitro refolding mechanism was extensively characterized via classical refolding experiments from a denaturant − as well as within cell-relevant environments. ,,,, The apoMb plasmid is codon-usage-optimized for expression in E. coli …”

Section: Resultsmentioning

confidence: 99%

Fluorescence Anisotropy Decays and Microscale-Volume Viscometry Reveal the Compaction of Ribosome-Bound Nascent Proteins

et al. 2021

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This work introduces a technology that combines fluorescence anisotropy decay with microscale-volume viscometry to investigate the compaction and dynamics of ribosome-bound nascent proteins. Protein folding in the cell, especially when nascent chains emerge from the ribosomal tunnel, is poorly understood. Previous investigations based on fluorescence anisotropy decay determined that a portion of the ribosome-bound nascent protein apomyoglobin (apoMb) forms a compact structure. This work, however, could not assess the size of the compact region. The combination of fluorescence anisotropy with microscale-volume viscometry, presented here, enables identifying the size of compact nascent-chain subdomains using a single fluorophore label. Our results demonstrate that the compact region of nascent apoMb contains 57–83 amino acids and lacks residues corresponding to the two native C-terminal helices. These amino acids are necessary for fully burying the nonpolar residues in the native structure, yet they are not available for folding before ribosome release. Therefore, apoMb requires a significant degree of post-translational folding for the generation of its native structure. In summary, the combination of fluorescence anisotropy decay and microscale-volume viscometry is a powerful approach to determine the size of independently tumbling compact regions of biomolecules. This technology is of general applicability to compact macromolecules linked to larger frameworks.

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Section: Resultsmentioning

confidence: 99%

Fluorescence Anisotropy Decays and Microscale-Volume Viscometry Reveal the Compaction of Ribosome-Bound Nascent Proteins

et al. 2021

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“…The transition between the native and denatured states of small globular proteins was initially considered a two-state process (two-state model of protein unfolding) [7][8][9]. Over the years, two generic folding intermediates were identified: the molten globule (MG) [10][11][12][13][14][15][16][17][18][19][20][21] and the pre-molten globule (PMG) [22][23][24][25][26]. Curiously, the existence of such folding intermediates was predicted in 1973 by Oleg B.…”

Section: Introductionmentioning

confidence: 99%

Pre-Molten, Wet, and Dry Molten Globules en Route to the Functional State of Proteins

Gupta

Uversky

2023

IJMS

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Transitions between the unfolded and native states of the ordered globular proteins are accompanied by the accumulation of several intermediates, such as pre-molten globules, wet molten globules, and dry molten globules. Structurally equivalent conformations can serve as native functional states of intrinsically disordered proteins. This overview captures the characteristics and importance of these molten globules in both structured and intrinsically disordered proteins. It also discusses examples of engineered molten globules. The formation of these intermediates under conditions of macromolecular crowding and their interactions with nanomaterials are also reviewed.

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“…The transition between the native and denatured states of small globular proteins was initially considered as a two-state process (two-state model of protein unfolding) [7][8][9]. Over the years, two generic folding intermediates were identified: the molten globule (MG) [10][11][12][13][14][15][16][17][18][19][20][21] and the pre-molten globule (PMG) [22][23][24][25][26]. Curiously, the existence of such folding intermediates was predicted in 1973 by Oleg B.…”

Section: Introductionmentioning

confidence: 99%

Pre-Molten, Wet, and Dry Molten Globules <i>En Route</i> to the Functional State of Proteins

Gupta¹,

Uversky²

2023

Preprint

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Transition between the unfolded and native states of the ordered globular proteins is accompanied by accumulation of several intermediates, such as pre-molten globule, wet molten globule, and dry molten globule. Structurally equivalent conformations can serve as native functional states of intrinsically disordered proteins. This overview captures the characteristics and importance of these molten globules in both structured and intrinsically disordered proteins. It also discusses examples of engineered molten globules. The formation of these intermediates under the conditions of macromolecular crowding and their interactions with nanomaterials are also reviewed.

show abstract

Intermediate states of apomyoglobin: Are they parts of the same area of conformations diagram?

Cited by 6 publications

References 27 publications

Fluorescence Anisotropy Decays and Microscale-Volume Viscometry Reveal the Compaction of Ribosome-Bound Nascent Proteins

Fluorescence Anisotropy Decays and Microscale-Volume Viscometry Reveal the Compaction of Ribosome-Bound Nascent Proteins

Pre-Molten, Wet, and Dry Molten Globules en Route to the Functional State of Proteins

Pre-Molten, Wet, and Dry Molten Globules <i>En Route</i> to the Functional State of Proteins

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