Beta sheets with a twist: the conformation of helical polyisocyanopeptides determined using vibrational circular dichroism

E. Schwartz; E. Schwartz; V. Liegeois; M. Koepf; P. Bodis; Jeroen Johannes Lambertus Maria Cornelissen; P. Brocorens; D. Beljonne; R.J.M. Nolte; A.E. Rowan; S. Woutersen; B. Champagne

doi:10.1002/chem.201300073

Beta sheets with a twist: the conformation of helical polyisocyanopeptides determined using vibrational circular dichroism

E. Schwartz, E. Schwartz, V. Liegeois, M. Koepf, P. Bodis, Jeroen Johannes Lambertus Maria Cornelissen, P. Brocorens, D. Beljonne, R.J.M. Nolte, A.E. Rowan, S. Woutersen, B. Champagne

Research output: Contribution to journal › Article › Academic › peer-review

15 Citations (Scopus)

Abstract

Detailed information on the architecture of polyisocyanopeptides based on vibrational circular dichroism (VCD) spectroscopy in combination with DFT calculations is presented. It is demonstrated that the screw sense of the helical polyisocyanides can be determined directly from the C[DOUBLE BOND]N-stretch vibrational region of the VCD spectrum. Analysis of the VCD signals associated with the amide I and amide II modes provides detailed information on the peptide side-chain arrangement in the polymer and indicates the presence of a helical β-sheet architecture, in which the dihedral angles are slightly different to those of natural β-sheet helices.

Original language	English
Pages (from-to)	13168-13174
Number of pages	6
Journal	Chemistry : a European journal
Volume	19
Issue number	39
DOIs	https://doi.org/10.1002/chem.201300073
Publication status	Published - 2013

Keywords

IR-90144
METIS-301670

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10.1002/chem.201300073

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Schwartz, E., Schwartz, E., Liegeois, V., Koepf, M., Bodis, P., Cornelissen, J. J. L. M., Brocorens, P., Beljonne, D., Nolte, R. J. M., Rowan, A. E., Woutersen, S., & Champagne, B. (2013). Beta sheets with a twist: the conformation of helical polyisocyanopeptides determined using vibrational circular dichroism. Chemistry : a European journal, 19(39), 13168-13174. https://doi.org/10.1002/chem.201300073

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title = "Beta sheets with a twist: the conformation of helical polyisocyanopeptides determined using vibrational circular dichroism",

abstract = "Detailed information on the architecture of polyisocyanopeptides based on vibrational circular dichroism (VCD) spectroscopy in combination with DFT calculations is presented. It is demonstrated that the screw sense of the helical polyisocyanides can be determined directly from the C[DOUBLE BOND]N-stretch vibrational region of the VCD spectrum. Analysis of the VCD signals associated with the amide I and amide II modes provides detailed information on the peptide side-chain arrangement in the polymer and indicates the presence of a helical β-sheet architecture, in which the dihedral angles are slightly different to those of natural β-sheet helices.",

keywords = "IR-90144, METIS-301670",

author = "E. Schwartz and E. Schwartz and V. Liegeois and M. Koepf and P. Bodis and Cornelissen, {Jeroen Johannes Lambertus Maria} and P. Brocorens and D. Beljonne and R.J.M. Nolte and A.E. Rowan and S. Woutersen and B. Champagne",

year = "2013",

doi = "10.1002/chem.201300073",

language = "English",

volume = "19",

pages = "13168--13174",

journal = "Chemistry : a European journal",

issn = "0947-6539",

publisher = "Wiley-VCH Verlag",

number = "39",

}

Schwartz, E, Schwartz, E, Liegeois, V, Koepf, M, Bodis, P, Cornelissen, JJLM, Brocorens, P, Beljonne, D, Nolte, RJM, Rowan, AE, Woutersen, S & Champagne, B 2013, 'Beta sheets with a twist: the conformation of helical polyisocyanopeptides determined using vibrational circular dichroism', Chemistry : a European journal, vol. 19, no. 39, pp. 13168-13174. https://doi.org/10.1002/chem.201300073

TY - JOUR

T1 - Beta sheets with a twist: the conformation of helical polyisocyanopeptides determined using vibrational circular dichroism

AU - Schwartz, E.

AU - Liegeois, V.

AU - Koepf, M.

AU - Bodis, P.

AU - Cornelissen, Jeroen Johannes Lambertus Maria

AU - Brocorens, P.

AU - Beljonne, D.

AU - Nolte, R.J.M.

AU - Rowan, A.E.

AU - Woutersen, S.

AU - Champagne, B.

PY - 2013

Y1 - 2013

N2 - Detailed information on the architecture of polyisocyanopeptides based on vibrational circular dichroism (VCD) spectroscopy in combination with DFT calculations is presented. It is demonstrated that the screw sense of the helical polyisocyanides can be determined directly from the C[DOUBLE BOND]N-stretch vibrational region of the VCD spectrum. Analysis of the VCD signals associated with the amide I and amide II modes provides detailed information on the peptide side-chain arrangement in the polymer and indicates the presence of a helical β-sheet architecture, in which the dihedral angles are slightly different to those of natural β-sheet helices.

AB - Detailed information on the architecture of polyisocyanopeptides based on vibrational circular dichroism (VCD) spectroscopy in combination with DFT calculations is presented. It is demonstrated that the screw sense of the helical polyisocyanides can be determined directly from the C[DOUBLE BOND]N-stretch vibrational region of the VCD spectrum. Analysis of the VCD signals associated with the amide I and amide II modes provides detailed information on the peptide side-chain arrangement in the polymer and indicates the presence of a helical β-sheet architecture, in which the dihedral angles are slightly different to those of natural β-sheet helices.

KW - IR-90144

KW - METIS-301670

U2 - 10.1002/chem.201300073

DO - 10.1002/chem.201300073

M3 - Article

VL - 19

SP - 13168

EP - 13174

JO - Chemistry : a European journal

JF - Chemistry : a European journal

SN - 0947-6539

IS - 39

ER -

Beta sheets with a twist: the conformation of helical polyisocyanopeptides determined using vibrational circular dichroism

Abstract

Keywords

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