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Hough, L. E.,Jung, H. T.,Krü,erke, D.,Heberling, M. S.,Nakata, M.,Jones, C. D.,Chen, D.,Link, D. R.,Zasadzinski, J.,Heppke, G.,Rabe, J. P.,Stocker, W.,Kö,rblova, E.,Walba, D. M.,Glaser, M. A. American Association for the Advancement of Scienc 2009 Science Vol.325 No.5939
<P>In the formation of chiral crystals, the tendency for twist in the orientation of neighboring molecules is incompatible with ordering into a lattice: Twist is expelled from planar layers at the expense of local strain. We report the ordered state of a neat material in which a local chiral structure is expressed as twisted layers, a state made possible by spatial limitation of layering to a periodic array of nanoscale filaments. Although made of achiral molecules, the layers in these filaments are twisted and rigorously homochiral--a broken symmetry. The precise structural definition achieved in filament self-assembly enables collective organization into arrays in which an additional broken symmetry--the appearance of macroscopic coherence of the filament twist--produces a liquid crystal phase of helically precessing layers.</P>
Radu, Ionela,Schleeger, Michael,Bolwien, Carsten,Heberle, Joachim Korean Society of Photoscience 2009 Photochemical & photobiological sciences Vol.8 No.11
The introduction of time-resolved Fourier transform infrared (FT-IR) spectroscopy to biochemistry opened the possibility of monitoring the catalytic mechanism of proteins along their reaction pathways. The infrared approach is very fruitful, particularly in the application to membrane proteins where NMR and X-ray crystallography are challenged by the size and protein hydrophobicity, as well as by their limited time-resolution. Here, we summarize the principles and experimental realizations of time-resolved FT-IR spectroscopy developed in our group and compare with aspects emerging from other laboratories. Examples of applications to retinal proteins and energy transduction complexes are reviewed, which emphasize the impact of time-resolved FT-IR spectroscopy on the understanding of protein reactions on the level of single bonds.