DOI: 10.1110/ps.8.6.1292. Study of the stability and unfolding mechanism of BBA1 by molecular dynamics simulations at different temperatures

Study of the stability and unfolding mechanism of BBA1 by molecular dynamics simulations at different temperatures

10.1110/ps.8.6.1292

Crossref journal-article

Wiley

Protein Science (311)

Abstract

AbstractBBA1 is a designed protein that has only 23 residues. It is the smallest protein without disulfide bridges that has a well‐defined tertiary structure in solution. We have performed unfolding molecular dynamics simulations on BBA1 and some of its mutants at 300, 330, 360, and 400 K to study their kinetic stability as well as the unfolding mechanism of BBA1. It was shown that the unfolding simulations can provide insights into the forces that stabilize the protein. Packing, hydrophobic interactions, and a salt bridge between Asp12 and Lys16 were found to be important to the protein' stability. The unfolding of BBA1 goes through two major steps: (1) disruption of the hydrophobic core and (2) unfolding of the helix. The β‐hairpin remains stable in the unfolding because of the high stability of the type II' turn connecting the two β‐strands.

Bibliography

Wang, L., Duan, Y., Shortle, R., Imperiali, B., & Kollman, P. A. (1999). Study of the stability and unfolding mechanism of BBA1 by molecular dynamics simulations at different temperatures. Protein Science, 8(6), 1292â1304. Portico.

Authors 5

Lu Wang (first)
Yong Duan (additional)
Rebecca Shortle (additional)
Barbara Imperiali (additional)
Peter A. Kollman (additional)

References 54 Referenced 46

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Dates

Type	When
Created	16 years, 6 months ago (Feb. 17, 2009, 5:03 p.m.)
Deposited	1 year, 10 months ago (Oct. 29, 2023, 5:29 a.m.)
Indexed	1 month, 3 weeks ago (July 11, 2025, 6:11 a.m.)
Issued	26 years, 8 months ago (Jan. 1, 1999)
Published	26 years, 8 months ago (Jan. 1, 1999)
Published Online	16 years, 8 months ago (Dec. 31, 2008)
Published Print	26 years, 8 months ago (Jan. 1, 1999)

Funders 0

None

BibTeX

@article{Wang_1999, title={Study of the stability and unfolding mechanism of BBA1 by molecular dynamics simulations at different temperatures}, volume={8}, ISSN={1469-896X}, url={http://dx.doi.org/10.1110/ps.8.6.1292}, DOI={10.1110/ps.8.6.1292}, number={6}, journal={Protein Science}, publisher={Wiley}, author={Wang, Lu and Duan, Yong and Shortle, Rebecca and Imperiali, Barbara and Kollman, Peter A.}, year={1999}, month=jan, pages={1292–1304} }

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