Synopses & Reviews
This book, the second volume in the "Springer Series in Biophysics", contains contributions to the conference on Biophysics and Synchrotron Radiation held in July 1986 at Frascati. It is devoted to advances in the resolution of biological molecule structure obtainable through synchroton radiation studies. Moreover, new perspectives are opened up by the future high brilliance synchroton radiation sources. The use of synchroton radiation has firmly established x-ray spectroscopy of biological molecules. More detailed knowledge on the local structure of active sites of metalloproteins, as well as a number of studies on the interaction of metal ions with other important biological macromolecular systems are presented. This new method for protein structure analysis is a major improvement for the rapidly expanding field of protein engineering.
This book the second volume in the "Springer Series in Biophysics" col- lects together contributions to the conference on "Biophysics and Syn- chrotron Radiation" held in July 86 at Frascati. This meeting addressed the advances on the structure of biological molecules obtained by using synchrotron radiation. In fact it was most timely to review the results of the research in biophysics which is rapidly developing at synchrotron radiation facilities. Moreover, there was interest to discuss the new perspectives opened up by the future high brilliance synchrotron radia- tion sources. With the use of synchrotron radiation, x-ray spectroscopy of biological molecules is firmly established in the techniques of EXAFS and XANES. Contributions to the detailed knowledge of local structure of active sites of metalloproteins by this approach are presented in this volume, together with a number of studies of -the interaction of metal ions with other important biological macromolecular systems. Structural determination of very large biological systems at high reso- lution, including a protein and its substrate, are reported. The experi- mental advances in protein crystallography presented here reduce the time for solving protein structures, thus satisfying a major require- ment of the rapidly-expanding field of protein engineering.
Table of Contents
Contents: X-Ray Diffraction.- X-Ray Spectroscopy.- X-Ray Scattering.- X-Ray Microscopy.- Time-Resolved Fluorescence.