%0 Book Section %1 statphys23_0419 %A Miura, Y. %A Sakashita, H. %A Cho, M. %A Cho, N. %B Abstract Book of the XXIII IUPAP International Conference on Statistical Physics %C Genova, Italy %D 2007 %E Pietronero, Luciano %E Loreto, Vittorio %E Zapperi, Stefano %K bonding helix-coil hydrogen melittin stability statphys23 thermal topic-10 transition %T Stability of helical structure and the helix-coil transition in a small peptide melittin %U http://st23.statphys23.org/webservices/abstract/preview_pop.php?ID_PAPER=419 %X It is known that bee venom melittin, a polypeptide of 26 amino acid residues, forms a helix in methanol and a random coil in a dilute aqueous solution at acidic pH1. The helical structure is stabilized mainly by intra-molecular hydrogen bonding. In a random coil state almost all hydrogen bonding in melittin are bonding between melittin and water molecules. To what extent are intra-molecular hydrogen bonding preserved in melittin in methanol/water mixed solvent? What conformation does melittin take in the mixed solvent? The purpose of our study is to experimentally elucidate correlation between intra-molecular hydrogen bonding and thermal stability of helix structure and to understand the mechanism of a helix-coil transition. The experiment was performed mainly by using 500MHz proton nuclear magnetic resonance (NMR) spectroscopy. To observe NMR signals of labile protons participating in intra-molecular hydrogen bonding melittin was dissolved in partially deuterated methanol (CD3OH)/ligh water (H2O) mixed solvent. We accumulated 2-dimensional NMR spectra at various temperatures to obtain information on strength of intra-molecular hydrogen bonding and helix content in melittin.\\ 1) R.Basso, et al., Eur. J. Biochem., 173, 136-146 (1988)

@incollection{statphys23_0419, abstract = {It is known that bee venom melittin, a polypeptide of 26 amino acid residues, forms a helix in methanol and a random coil in a dilute aqueous solution at acidic pH[1]. The helical structure is stabilized mainly by intra-molecular hydrogen bonding. In a random coil state almost all hydrogen bonding in melittin are bonding between melittin and water molecules. To what extent are intra-molecular hydrogen bonding preserved in melittin in methanol/water mixed solvent? What conformation does melittin take in the mixed solvent? The purpose of our study is to experimentally elucidate correlation between intra-molecular hydrogen bonding and thermal stability of helix structure and to understand the mechanism of a helix-coil transition. The experiment was performed mainly by using 500MHz proton nuclear magnetic resonance (NMR) spectroscopy. To observe NMR signals of labile protons participating in intra-molecular hydrogen bonding melittin was dissolved in partially deuterated methanol (CD3OH)/ligh water (H2O) mixed solvent. We accumulated 2-dimensional NMR spectra at various temperatures to obtain information on strength of intra-molecular hydrogen bonding and helix content in melittin.\\ 1) R.Basso, et al., Eur. J. Biochem., 173, 136-146 (1988)}, added-at = {2007-06-20T10:16:09.000+0200}, address = {Genova, Italy}, author = {Miura, Y. and Sakashita, H. and Cho, M. and Cho, N.}, biburl = {https://www.bibsonomy.org/bibtex/29f4cea1a086d7f609c7665a323f24e87/statphys23}, booktitle = {Abstract Book of the XXIII IUPAP International Conference on Statistical Physics}, editor = {Pietronero, Luciano and Loreto, Vittorio and Zapperi, Stefano}, interhash = {120ac3b01667d290e35fb4578763286e}, intrahash = {9f4cea1a086d7f609c7665a323f24e87}, keywords = {bonding helix-coil hydrogen melittin stability statphys23 thermal topic-10 transition}, month = {9-13 July}, timestamp = {2007-06-20T10:16:19.000+0200}, title = {Stability of helical structure and the helix-coil transition in a small peptide melittin}, url = {http://st23.statphys23.org/webservices/abstract/preview_pop.php?ID_PAPER=419}, year = 2007 }