The influence of a chiral amino acid on the helical handedness of PNA in solution and in crystals

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

The influence of a chiral amino acid on the helical handedness of PNA in solution and in crystals. / Rasmussen, Hanne B.; Liljefors, T; Petersson, B; Nielsen, P E; Liljefors, T; Kastrup, Jette Sandholm Jensen.

In: Journal of Biomolecular Structure & Dynamics, Vol. 21, No. 4, 02.2004, p. 495-502.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Rasmussen, HB, Liljefors, T, Petersson, B, Nielsen, PE, Liljefors, T & Kastrup, JSJ 2004, 'The influence of a chiral amino acid on the helical handedness of PNA in solution and in crystals', Journal of Biomolecular Structure & Dynamics, vol. 21, no. 4, pp. 495-502. https://doi.org/10.1080/07391102.2004.10506943

APA

Rasmussen, H. B., Liljefors, T., Petersson, B., Nielsen, P. E., Liljefors, T., & Kastrup, J. S. J. (2004). The influence of a chiral amino acid on the helical handedness of PNA in solution and in crystals. Journal of Biomolecular Structure & Dynamics, 21(4), 495-502. https://doi.org/10.1080/07391102.2004.10506943

Vancouver

Rasmussen HB, Liljefors T, Petersson B, Nielsen PE, Liljefors T, Kastrup JSJ. The influence of a chiral amino acid on the helical handedness of PNA in solution and in crystals. Journal of Biomolecular Structure & Dynamics. 2004 Feb;21(4):495-502. https://doi.org/10.1080/07391102.2004.10506943

Author

Rasmussen, Hanne B. ; Liljefors, T ; Petersson, B ; Nielsen, P E ; Liljefors, T ; Kastrup, Jette Sandholm Jensen. / The influence of a chiral amino acid on the helical handedness of PNA in solution and in crystals. In: Journal of Biomolecular Structure & Dynamics. 2004 ; Vol. 21, No. 4. pp. 495-502.

Bibtex

@article{5c782fbff678459da3f7f591c59dc83a,
title = "The influence of a chiral amino acid on the helical handedness of PNA in solution and in crystals",
abstract = "The X-ray structure of a self-complementary PNA hexamer (H-CGTACG-L-Lys-NH(2)) has been determined to 2.35 A resolution. The introduction of an L-lysine moiety has previously been shown to induce a preferred left-handedness of the PNA double helices in aqueous solution. However, in the crystal structure an equal amount of interchanging right- and left-handed helices is observed. The lysine moieties are pointing into large solvent channels and no significant interactions between this moiety and the remaining PNA molecule are observed. In contrast, molecular mechanics calculations show a preference for the left-handed helix of this hexameric PNA in aqueous solution as expected. The calculations indicate that the difference in the free energy of solvation between the left-handed and the right-handed helix is the determining factor for the preference of the left-handed helix in aqueous solution.",
keywords = "Amino Acids, Computer Simulation, Crystallography, X-Ray, Lysine, Models, Molecular, Nucleic Acid Conformation, Peptide Nucleic Acids, Thermodynamics",
author = "Rasmussen, {Hanne B.} and T Liljefors and B Petersson and Nielsen, {P E} and T Liljefors and Kastrup, {Jette Sandholm Jensen}",
year = "2004",
month = "2",
doi = "10.1080/07391102.2004.10506943",
language = "English",
volume = "21",
pages = "495--502",
journal = "Journal of Biomolecular Structure & Dynamics",
issn = "0739-1102",
publisher = "Taylor & Francis",
number = "4",

}

RIS

TY - JOUR

T1 - The influence of a chiral amino acid on the helical handedness of PNA in solution and in crystals

AU - Rasmussen, Hanne B.

AU - Liljefors, T

AU - Petersson, B

AU - Nielsen, P E

AU - Liljefors, T

AU - Kastrup, Jette Sandholm Jensen

PY - 2004/2

Y1 - 2004/2

N2 - The X-ray structure of a self-complementary PNA hexamer (H-CGTACG-L-Lys-NH(2)) has been determined to 2.35 A resolution. The introduction of an L-lysine moiety has previously been shown to induce a preferred left-handedness of the PNA double helices in aqueous solution. However, in the crystal structure an equal amount of interchanging right- and left-handed helices is observed. The lysine moieties are pointing into large solvent channels and no significant interactions between this moiety and the remaining PNA molecule are observed. In contrast, molecular mechanics calculations show a preference for the left-handed helix of this hexameric PNA in aqueous solution as expected. The calculations indicate that the difference in the free energy of solvation between the left-handed and the right-handed helix is the determining factor for the preference of the left-handed helix in aqueous solution.

AB - The X-ray structure of a self-complementary PNA hexamer (H-CGTACG-L-Lys-NH(2)) has been determined to 2.35 A resolution. The introduction of an L-lysine moiety has previously been shown to induce a preferred left-handedness of the PNA double helices in aqueous solution. However, in the crystal structure an equal amount of interchanging right- and left-handed helices is observed. The lysine moieties are pointing into large solvent channels and no significant interactions between this moiety and the remaining PNA molecule are observed. In contrast, molecular mechanics calculations show a preference for the left-handed helix of this hexameric PNA in aqueous solution as expected. The calculations indicate that the difference in the free energy of solvation between the left-handed and the right-handed helix is the determining factor for the preference of the left-handed helix in aqueous solution.

KW - Amino Acids

KW - Computer Simulation

KW - Crystallography, X-Ray

KW - Lysine

KW - Models, Molecular

KW - Nucleic Acid Conformation

KW - Peptide Nucleic Acids

KW - Thermodynamics

U2 - 10.1080/07391102.2004.10506943

DO - 10.1080/07391102.2004.10506943

M3 - Journal article

C2 - 14692794

VL - 21

SP - 495

EP - 502

JO - Journal of Biomolecular Structure & Dynamics

JF - Journal of Biomolecular Structure & Dynamics

SN - 0739-1102

IS - 4

ER -

ID: 44729739