VCD spectroscopic properties of the beta-hairpin forming miniprotein CLN025 in various solvents.

Biopolymers
Marcus P D HatfieldSándor Lovas

Abstract

Electronic and vibrational circular dichroism are often used to determine the secondary structure of proteins, because each secondary structure has a unique spectrum. Little is known about the vibrational circular dichroic spectroscopic features of the beta-hairpin. In this study, the VCD spectral features of a decapeptide, YYDPETGTWY (CLN025), which forms a stable beta-hairpin that is stabilized by intramolecular weakly polar interactions and hydrogen bonds were determined. Molecular dynamics simulations and ECD spectropolarimetry were used to confirm that CLN025 adopts a beta-hairpin in water, TFE, MeOH, and DMSO and to examine differences in the secondary structure, hydrogen bonds, and weakly polar interactions. CLN025 was synthesized by microwave-assisted solid phase peptide synthesis with N(alpha)-Fmoc protected amino acids. The VCD spectra displayed a (-,+,-) pattern with bands at 1640 to 1656 cm(-1), 1667 to 1687 cm(-1), and 1679 to 1686 cm(-1) formed by the overlap of a lower frequency negative couplet and a higher frequency positive couplet. A maximum IR absorbance was observed at 1647 to 1663 cm(-1) with component bands at 1630 cm(-1), 1646 cm(-1), 1658 cm(-1), and 1675 to 1680 cm(-1) that are indicative of the beta-s...Continue Reading

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Citations

Apr 13, 2011·The Journal of Physical Chemistry. B·Marcus P D HatfieldSándor Lovas
Feb 13, 2010·The Journal of Physical Chemistry. B·Marcus P D HatfieldSándor Lovas
Oct 21, 2011·Chemical Society Reviews·Søren L PedersenKnud J Jensen
May 7, 2013·The Journal of Physical Chemistry. B·Sándor LovasYuri L Lyubchenko
Apr 20, 2013·The Journal of Physical Chemistry. B·Panagiota S Georgoulia, Nicholas M Glykos
Nov 10, 2010·Langmuir : the ACS Journal of Surfaces and Colloids·Annette F Dexter
Jan 26, 2022·Organic & Biomolecular Chemistry·Maria A S YokomichiJoao M Batista

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