MISC

2006年8月

Electronic and vibrational circular dichroism of aromatic amino acids by density functional theory

CHIRALITY
  • Takeyuki Tanaka
  • ,
  • Takashi S. Kodama
  • ,
  • Hayato E. Morita
  • ,
  • Takashi Ohno

18
8
開始ページ
652
終了ページ
661
記述言語
英語
掲載種別
DOI
10.1002/chir.20277
出版者・発行元
WILEY-LISS

Structures of model compounds mimicking aromatic amino acid residues in proteins are optimized by density functional theory (DFT), assuming that the main-chain conformation was a random coil. Excitation energies and dipole and rotational strengths for the optimized structures were calculated based on time-dependent DFT (TD-DFT). The electronic circular dichroism (ECD) bands of the models were significantly affected by side-chain conformations. Hydration models of the aromatic residues were also subjected to TD-DFT calculations, and the ECD bands of these models were found to be highly perturbed by the hydration of the main-chain amide groups. In addition to calculating the random-coil conformation, we also performed TD-DFT calculations of the aromatic residue models, assuming that the main-chain conformation was an a-helix or beta-strand. As expected, the overall feature of the ECD bands was also perturbed by the main-chain conformations. Moreover, vibrational circular dichroism (VCD) spectra of the hydration models in a random-coil structure were simulated by DFT, which showed that the VCD spectra are more sensitive to the side-chain conformations than the ECD spectra. The present results show that analyses combining ECD and VCD spectroscopy and using DFT calculations can elucidate the main- and side-chain conformations of aromatic residues in proteins.

Web of Science ® 被引用回数 : 14

リンク情報
DOI
https://doi.org/10.1002/chir.20277
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000239204000011&DestApp=WOS_CPL

エクスポート
BibTeX RIS