Evidences of a natively unfolded state for the human topoisomerase IB N-terminal domain

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Evidences of a natively unfolded state for the human topoisomerase IB N-terminal domain. / Vassallo, Oscar; Castelli, Silvia; D'Annessa, Ilda; della Rocca, Blsco Morozzo; Stella, Lorenzo; Knudsen, Birgitta R.; Desideri, Alessandro.

In: Amino Acids, Vol. 41, No. 4, 01.10.2011, p. 945-953.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Vassallo, O, Castelli, S, D'Annessa, I, della Rocca, BM, Stella, L, Knudsen, BR & Desideri, A 2011, 'Evidences of a natively unfolded state for the human topoisomerase IB N-terminal domain', Amino Acids, vol. 41, no. 4, pp. 945-953. https://doi.org/10.1007/s00726-010-0794-x

APA

Vassallo, O., Castelli, S., D'Annessa, I., della Rocca, B. M., Stella, L., Knudsen, B. R., & Desideri, A. (2011). Evidences of a natively unfolded state for the human topoisomerase IB N-terminal domain. Amino Acids, 41(4), 945-953. https://doi.org/10.1007/s00726-010-0794-x

CBE

Vassallo O, Castelli S, D'Annessa I, della Rocca BM, Stella L, Knudsen BR, Desideri A. 2011. Evidences of a natively unfolded state for the human topoisomerase IB N-terminal domain. Amino Acids. 41(4):945-953. https://doi.org/10.1007/s00726-010-0794-x

MLA

Vancouver

Vassallo O, Castelli S, D'Annessa I, della Rocca BM, Stella L, Knudsen BR et al. Evidences of a natively unfolded state for the human topoisomerase IB N-terminal domain. Amino Acids. 2011 Oct 1;41(4):945-953. https://doi.org/10.1007/s00726-010-0794-x

Author

Vassallo, Oscar ; Castelli, Silvia ; D'Annessa, Ilda ; della Rocca, Blsco Morozzo ; Stella, Lorenzo ; Knudsen, Birgitta R. ; Desideri, Alessandro. / Evidences of a natively unfolded state for the human topoisomerase IB N-terminal domain. In: Amino Acids. 2011 ; Vol. 41, No. 4. pp. 945-953.

Bibtex

@article{655e4a2f8a5841b4b595cc23815a77e1,
title = "Evidences of a natively unfolded state for the human topoisomerase IB N-terminal domain",
abstract = "The N-terminal domain of human topoisomerase IB has been expressed, purified and characterized by spectroscopic techniques. CD spectra as a function of concentration and pH indicate that the domain does not possess any defined secondary structure. The protein is probably in a natively unfolded state since its denaturation curve is indicative of a non-cooperative transition. Evidence of a partially folded structure comes from the fluorescence spectrum of ANS, whose intensity increases in presence of the domain. Indication of a partial structural arrangement of the domain comes also from the endogenous fluorescence of tryptophans that is centred at 350 nm in the native and shifts to 354 nm in the fully denaturated protein. Interestingly despite the poor structural degree, as also confirmed by a predictive approach, the domain efficiently binds DNA, suggesting that the absence of a defined 3D structure has a functional meaning that permits the domain to be available for the interaction with different molecular partners.",
author = "Oscar Vassallo and Silvia Castelli and Ilda D'Annessa and {della Rocca}, {Blsco Morozzo} and Lorenzo Stella and Knudsen, {Birgitta R.} and Alessandro Desideri",
note = "Copyright 2012 Elsevier B.V., All rights reserved.",
year = "2011",
month = "10",
day = "1",
doi = "10.1007/s00726-010-0794-x",
language = "English",
volume = "41",
pages = "945--953",
journal = "Amino Acids",
issn = "0939-4451",
publisher = "Springer Wien",
number = "4",

}

RIS

TY - JOUR

T1 - Evidences of a natively unfolded state for the human topoisomerase IB N-terminal domain

AU - Vassallo, Oscar

AU - Castelli, Silvia

AU - D'Annessa, Ilda

AU - della Rocca, Blsco Morozzo

AU - Stella, Lorenzo

AU - Knudsen, Birgitta R.

AU - Desideri, Alessandro

N1 - Copyright 2012 Elsevier B.V., All rights reserved.

PY - 2011/10/1

Y1 - 2011/10/1

N2 - The N-terminal domain of human topoisomerase IB has been expressed, purified and characterized by spectroscopic techniques. CD spectra as a function of concentration and pH indicate that the domain does not possess any defined secondary structure. The protein is probably in a natively unfolded state since its denaturation curve is indicative of a non-cooperative transition. Evidence of a partially folded structure comes from the fluorescence spectrum of ANS, whose intensity increases in presence of the domain. Indication of a partial structural arrangement of the domain comes also from the endogenous fluorescence of tryptophans that is centred at 350 nm in the native and shifts to 354 nm in the fully denaturated protein. Interestingly despite the poor structural degree, as also confirmed by a predictive approach, the domain efficiently binds DNA, suggesting that the absence of a defined 3D structure has a functional meaning that permits the domain to be available for the interaction with different molecular partners.

AB - The N-terminal domain of human topoisomerase IB has been expressed, purified and characterized by spectroscopic techniques. CD spectra as a function of concentration and pH indicate that the domain does not possess any defined secondary structure. The protein is probably in a natively unfolded state since its denaturation curve is indicative of a non-cooperative transition. Evidence of a partially folded structure comes from the fluorescence spectrum of ANS, whose intensity increases in presence of the domain. Indication of a partial structural arrangement of the domain comes also from the endogenous fluorescence of tryptophans that is centred at 350 nm in the native and shifts to 354 nm in the fully denaturated protein. Interestingly despite the poor structural degree, as also confirmed by a predictive approach, the domain efficiently binds DNA, suggesting that the absence of a defined 3D structure has a functional meaning that permits the domain to be available for the interaction with different molecular partners.

UR - http://www.scopus.com/inward/record.url?scp=83255184524&partnerID=8YFLogxK

U2 - 10.1007/s00726-010-0794-x

DO - 10.1007/s00726-010-0794-x

M3 - Journal article

VL - 41

SP - 945

EP - 953

JO - Amino Acids

JF - Amino Acids

SN - 0939-4451

IS - 4

ER -