DOI: 10.1073/pnas.0407982102. Specific collapse followed by slow hydrogen-bond formation of β-sheet in the folding of single-chain monellin

Specific collapse followed by slow hydrogen-bond formation of β-sheet in the folding of single-chain monellin

10.1073/pnas.0407982102

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

Characterization of the conformational landscapes for proteins with different secondary structures is important in elucidating the mechanism of protein folding. The folding trajectory of single-chain monellin composed of a five-stranded β-sheet and a helix was investigated by using a pH-jump from the alkaline unfolded to native state. The kinetic changes in the secondary structures and in the overall size and shape were measured by circular dichroism spectroscopy and small-angle x-ray scattering, respectively. The formation of the tertiary structure was monitored by intrinsic and extrinsic fluorescence. A significant collapse was observed within 300 μs after the pH-jump, leading to the intermediate with a small amount of secondary and tertiary structures but with an overall oblate shape. Subsequently, the stepwise formation of secondary and tertiary structures was detected. The current observation was consistent with the theoretical prediction that a more significant collapse precedes the formation of secondary structures in the folding of β-sheet proteins than that of helical proteins [Shea, J. E., Onuchic, J. N. & Brooks, C. L., III (2002) Proc. Natl. Acad. Sci. USA 99, 16064–16068]. Furthermore, it was implied that the initial collapse was promoted by the formation of some specific structural elements, such as tight turns, to form the oblate shape.

Bibliography

Kimura, T., Uzawa, T., Ishimori, K., Morishima, I., Takahashi, S., Konno, T., Akiyama, S., & Fujisawa, T. (2005). Specific collapse followed by slow hydrogen-bond formation of Î²-sheet in the folding of single-chain monellin. Proceedings of the National Academy of Sciences, 102(8), 2748â2753.

Authors 8

Tetsunari Kimura (first)
Takanori Uzawa (additional)
Koichiro Ishimori (additional)
Isao Morishima (additional)
Satoshi Takahashi (additional)
Takashi Konno (additional)
Shuji Akiyama (additional)
Tetsuro Fujisawa (additional)

References 51 Referenced 87

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Dates

Type	When
Created	20 years, 6 months ago (Feb. 14, 2005, 8:24 p.m.)
Deposited	3 years, 4 months ago (April 12, 2022, 10:11 a.m.)
Indexed	1 month ago (July 30, 2025, 10:28 a.m.)
Issued	20 years, 6 months ago (Feb. 14, 2005)
Published	20 years, 6 months ago (Feb. 14, 2005)
Published Online	20 years, 6 months ago (Feb. 14, 2005)
Published Print	20 years, 6 months ago (Feb. 22, 2005)

Funders 0

None

BibTeX

@article{Kimura_2005, title={Specific collapse followed by slow hydrogen-bond formation of β-sheet in the folding of single-chain monellin}, volume={102}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.0407982102}, DOI={10.1073/pnas.0407982102}, number={8}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Kimura, Tetsunari and Uzawa, Takanori and Ishimori, Koichiro and Morishima, Isao and Takahashi, Satoshi and Konno, Takashi and Akiyama, Shuji and Fujisawa, Tetsuro}, year={2005}, month=feb, pages={2748–2753} }

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