%0 Book Section %1 statphys23_0361 %A Sakashita, H. %A Miuya, Y. %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 heat hydrogen latent phase sol-gel statphys23 topic-10 transition %T Thermal Melting of Triple Helices and Hydrogen Bonding in Collagen Model Peptides (Pro-Pro-Gly)$_5$ and (Pro-Hyp-Gly)$_5$ %U http://st23.statphys23.org/webservices/abstract/preview_pop.php?ID_PAPER=361 %X A small rod like molecule of collagen model peptide (Pro-Pro-Gly)$_5$ and (Pro-Hyp-Gly)$_5$, with molecular length 6nm, form triple helices in acqueous solution at room temperarute, and undergoes thermal melting (from triple helices to three coils) around 20C, accompanied with the latent heat and the breaking of 15 hydrogen bonding between intra-chains(triple helices). In contrast with the other model peptide such as (Pro-Pro-Gly)$_10$ and (Pro-Hyp-Gly)$_10$ with more long molecular length, in these system there is no crystal formation ( as an asemble of triple helices) at room temperature, which prevents precise observation of the hydrogen bonded protons. Hydrogen bonding is a main stabilization force for 3-dimentional structure of proteins.Our purpose is to understand the fundamental behavior of hydrogen bonding in these simple systems: what is the formation/breaking of the hydrogen bonding; what is the microscopic origin of the latent heat. We have investigated the temperarure dependence of the hydrogen bonded NH proton signals by using gCOSY and wet-TOCSY 500MHz NMR spectroscopy and thermal analysis(DSC).

@incollection{statphys23_0361, abstract = {A small rod like molecule of collagen model peptide (Pro-Pro-Gly)$_5$ and (Pro-Hyp-Gly)$_5$, with molecular length 6nm, form triple helices in acqueous solution at room temperarute, and undergoes thermal melting (from triple helices to three coils) around 20C, accompanied with the latent heat and the breaking of 15 hydrogen bonding between intra-chains(triple helices). In contrast with the other model peptide such as (Pro-Pro-Gly)$_10$ and (Pro-Hyp-Gly)$_10$ with more long molecular length, in these system there is no crystal formation ( as an asemble of triple helices) at room temperature, which prevents precise observation of the hydrogen bonded protons. Hydrogen bonding is a main stabilization force for 3-dimentional structure of proteins.Our purpose is to understand the fundamental behavior of hydrogen bonding in these simple systems: what is the formation/breaking of the hydrogen bonding; what is the microscopic origin of the latent heat. We have investigated the temperarure dependence of the hydrogen bonded NH proton signals by using gCOSY and wet-TOCSY 500MHz NMR spectroscopy and thermal analysis(DSC).}, added-at = {2007-06-20T10:16:09.000+0200}, address = {Genova, Italy}, author = {Sakashita, H. and Miuya, Y. and Cho, M. and Cho, N.}, biburl = {https://www.bibsonomy.org/bibtex/23f0e6c57b2d5dac5a0279edae11de3e0/statphys23}, booktitle = {Abstract Book of the XXIII IUPAP International Conference on Statistical Physics}, editor = {Pietronero, Luciano and Loreto, Vittorio and Zapperi, Stefano}, interhash = {61e05abcc33125c8252a6086104d22f0}, intrahash = {3f0e6c57b2d5dac5a0279edae11de3e0}, keywords = {bonding heat hydrogen latent phase sol-gel statphys23 topic-10 transition}, month = {9-13 July}, timestamp = {2007-06-20T10:16:18.000+0200}, title = {Thermal Melting of Triple Helices and Hydrogen Bonding in Collagen Model Peptides (Pro-Pro-Gly)$_5$ and (Pro-Hyp-Gly)$_5$}, url = {http://st23.statphys23.org/webservices/abstract/preview_pop.php?ID_PAPER=361}, year = 2007 }