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 β-hairpin. In this study, the VCD spectral features of a decapeptide, YYDPETGTWY (CLN025), which forms a stable β-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 β-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 Nα-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 β-sheet, random meander, either random meander or loop and turn, respectively. These results are similar to the results of others, who examined the VCD spectra of β-hairpins formed by DPro-Xxx turns and indicated that observed pattern is typical of β-hairpins.
| Original language | English |
|---|---|
| Pages (from-to) | 442-450 |
| Number of pages | 9 |
| Journal | Biopolymers |
| Volume | 93 |
| Issue number | 5 |
| DOIs | |
| State | Published - May 2010 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Biophysics
- Biomaterials
- Organic Chemistry
Cite this
VCD spectroscopic properties of the β-hairpin forming miniprotein CLN025 in various solvents. / Hatfield, Marcus P D; Murphy, Richard F.; Lovas, Sándor.
In: Biopolymers, Vol. 93, No. 5, 05.2010, p. 442-450.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - VCD spectroscopic properties of the β-hairpin forming miniprotein CLN025 in various solvents
AU - Hatfield, Marcus P D
AU - Murphy, Richard F.
AU - Lovas, Sándor
PY - 2010/5
Y1 - 2010/5
N2 - 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 β-hairpin. In this study, the VCD spectral features of a decapeptide, YYDPETGTWY (CLN025), which forms a stable β-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 β-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 Nα-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 β-sheet, random meander, either random meander or loop and turn, respectively. These results are similar to the results of others, who examined the VCD spectra of β-hairpins formed by DPro-Xxx turns and indicated that observed pattern is typical of β-hairpins.
AB - 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 β-hairpin. In this study, the VCD spectral features of a decapeptide, YYDPETGTWY (CLN025), which forms a stable β-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 β-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 Nα-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 β-sheet, random meander, either random meander or loop and turn, respectively. These results are similar to the results of others, who examined the VCD spectra of β-hairpins formed by DPro-Xxx turns and indicated that observed pattern is typical of β-hairpins.
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UR - http://www.scopus.com/inward/citedby.url?scp=77951951722&partnerID=8YFLogxK
U2 - 10.1002/bip.21356
DO - 10.1002/bip.21356
M3 - Article
C2 - 19937759
AN - SCOPUS:77951951722
VL - 93
SP - 442
EP - 450
JO - Biopolymers
JF - Biopolymers
SN - 0006-3525
IS - 5
ER -