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Steffen Petersen

Trehalose favors a cutinase compact intermediate off-folding pathway

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Standard

Trehalose favors a cutinase compact intermediate off-folding pathway. / Melo, Eduardo P.; Chen, Lu Yang; Cabral, Joaquim M.S.; Fojan, Peter; Petersen, Steffen B.; Otzen, Daniel E.

I: Biochemistry, Bind 42, Nr. 24, 24.06.2003, s. 7611-7617.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Melo, EP, Chen, LY, Cabral, JMS, Fojan, P, Petersen, SB & Otzen, DE 2003, 'Trehalose favors a cutinase compact intermediate off-folding pathway', Biochemistry, bind 42, nr. 24, s. 7611-7617. https://doi.org/10.1021/bi034267x

APA

Melo, E. P., Chen, L. Y., Cabral, J. M. S., Fojan, P., Petersen, S. B., & Otzen, D. E. (2003). Trehalose favors a cutinase compact intermediate off-folding pathway. Biochemistry, 42(24), 7611-7617. https://doi.org/10.1021/bi034267x

CBE

MLA

Vancouver

Melo EP, Chen LY, Cabral JMS, Fojan P, Petersen SB, Otzen DE. Trehalose favors a cutinase compact intermediate off-folding pathway. Biochemistry. 2003 jun 24;42(24):7611-7617. https://doi.org/10.1021/bi034267x

Author

Melo, Eduardo P. ; Chen, Lu Yang ; Cabral, Joaquim M.S. ; Fojan, Peter ; Petersen, Steffen B. ; Otzen, Daniel E. / Trehalose favors a cutinase compact intermediate off-folding pathway. I: Biochemistry. 2003 ; Bind 42, Nr. 24. s. 7611-7617.

Bibtex

@article{116588668b44487690310522e8df7b09,
title = "Trehalose favors a cutinase compact intermediate off-folding pathway",
abstract = "The folding of cutinase, an enzyme displaying lipolytic activity, has been studied in the presence of trehalose. Equilibrium unfolding data show that trehalose increases the free energy change between folded and unfolded states. Unfolding kinetics reveal the presence of an intermediate which is ca. 60% folded in terms of solvent exposure. Trehalose stabilizes this intermediate relative to the folded state. In contrast, the intermediate revealed by folding kinetics is more compact than the transition state, as shown by the positive slope observed at low denaturant concentration in the chevron plot, as well as the decrease in the observable rate constant for folding with the increase in trehalose concentration. This intermediate displays more than 50% of area buried from the solvent (relative to the native state) compared to around 40% for the transition state for folding and therefore appears to be off the folding pathway. Trehalose stabilizes and guanidine hydrochloride destabilizes this compact intermediate. Both unfolding and folding kinetics show that compact conformational states are stabilized by trehalose, in agreement with current models on the effect of compatible solutes. This effect occurs even for compact states that decelerate the folding as in the case of the intermediate revealed by folding kinetics.",
author = "Melo, {Eduardo P.} and Chen, {Lu Yang} and Cabral, {Joaquim M.S.} and Peter Fojan and Petersen, {Steffen B.} and Otzen, {Daniel E.}",
year = "2003",
month = jun,
day = "24",
doi = "10.1021/bi034267x",
language = "English",
volume = "42",
pages = "7611--7617",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "ACS Publications",
number = "24",

}

RIS

TY - JOUR

T1 - Trehalose favors a cutinase compact intermediate off-folding pathway

AU - Melo, Eduardo P.

AU - Chen, Lu Yang

AU - Cabral, Joaquim M.S.

AU - Fojan, Peter

AU - Petersen, Steffen B.

AU - Otzen, Daniel E.

PY - 2003/6/24

Y1 - 2003/6/24

N2 - The folding of cutinase, an enzyme displaying lipolytic activity, has been studied in the presence of trehalose. Equilibrium unfolding data show that trehalose increases the free energy change between folded and unfolded states. Unfolding kinetics reveal the presence of an intermediate which is ca. 60% folded in terms of solvent exposure. Trehalose stabilizes this intermediate relative to the folded state. In contrast, the intermediate revealed by folding kinetics is more compact than the transition state, as shown by the positive slope observed at low denaturant concentration in the chevron plot, as well as the decrease in the observable rate constant for folding with the increase in trehalose concentration. This intermediate displays more than 50% of area buried from the solvent (relative to the native state) compared to around 40% for the transition state for folding and therefore appears to be off the folding pathway. Trehalose stabilizes and guanidine hydrochloride destabilizes this compact intermediate. Both unfolding and folding kinetics show that compact conformational states are stabilized by trehalose, in agreement with current models on the effect of compatible solutes. This effect occurs even for compact states that decelerate the folding as in the case of the intermediate revealed by folding kinetics.

AB - The folding of cutinase, an enzyme displaying lipolytic activity, has been studied in the presence of trehalose. Equilibrium unfolding data show that trehalose increases the free energy change between folded and unfolded states. Unfolding kinetics reveal the presence of an intermediate which is ca. 60% folded in terms of solvent exposure. Trehalose stabilizes this intermediate relative to the folded state. In contrast, the intermediate revealed by folding kinetics is more compact than the transition state, as shown by the positive slope observed at low denaturant concentration in the chevron plot, as well as the decrease in the observable rate constant for folding with the increase in trehalose concentration. This intermediate displays more than 50% of area buried from the solvent (relative to the native state) compared to around 40% for the transition state for folding and therefore appears to be off the folding pathway. Trehalose stabilizes and guanidine hydrochloride destabilizes this compact intermediate. Both unfolding and folding kinetics show that compact conformational states are stabilized by trehalose, in agreement with current models on the effect of compatible solutes. This effect occurs even for compact states that decelerate the folding as in the case of the intermediate revealed by folding kinetics.

UR - http://www.scopus.com/inward/record.url?scp=0038070096&partnerID=8YFLogxK

U2 - 10.1021/bi034267x

DO - 10.1021/bi034267x

M3 - Journal article

C2 - 12809518

AN - SCOPUS:0038070096

VL - 42

SP - 7611

EP - 7617

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 24

ER -