The influence of a chiral amino acid on the helical handedness of PNA in solution and in crystals
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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 journal › Journal article › Research › peer-review
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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 and Dynamics
JF - Journal of Biomolecular Structure and Dynamics
SN - 0739-1102
IS - 4
ER -
ID: 44729739