This volume collects a number of the invited lectures and a few selected contrib utions presented at the International Symposium on Structure and Dynamics of Nucleic Acids, Proteins and Membranes held August 31st through September 5th, 1986, in Riva del Garda, Italy. The title of the conference as well as a number of the topics covered represent a continuation of two previous conferences, the first held in 1982 at the University of California in San Diego, and the second in 1984 in Rome at the Accademia dei Lincei. These two earlier conferences have been documented in Structure and Dynamics: Nucleic Acids and Proteins, edited by E. Clementi and R. H. Sarma, Adenine Press, New York, 1983, and Structure and Motion: Membranes, Nucleic Acids and Proteins, edited by E. Clementi, G. Corongiu, M. H. Sarma and R. H. Sarma, Adenine Press, New York, 1985. At this conference in Riva del Garda we were very hesitant to keep the name of the conference the same as the two previous ones. Indeed, a number of topics discussed in this conference were not included in the previous ones and even the emphasis of this gathering is only partly reflected in the conference title. An alternative title would have been Structure and Dynamics of Nucleic Acids, Proteins, and Higher Functions, or, possibly, "higher components" rather than "higher functions.

Studying the structural dynamics of biomolecules is a challenging problem that has received much attention due to the recognition that structurally, most native biomolecules exist as ensemble of heterogenous states that inter-convert on the time scales rang- ing from nanoseconds to seconds. The implication of this is far reaching affecting all cellular process that rely on biomolecular recognition and interaction. Central to understanding how biomolecules function within this paradigm is the ability to determine structural ensembles of a target system. Equally important is the task of determining the rates of conformational transitions. Here I present application and validation of an approach that have the potential to characterize the structural en- sembles of highly flexible ribonucleic acids (RNAs) by combining molecular dynamics (MD) simulations and nuclear magnetic resonance (NMR) spectroscopy. As a special topic, a method is presented that can be used to extract rates of conformational transitions from MD simulations.

This book is a self-contained introduction to the theory of atomic motion in proteins and nucleic acids. An understanding of such motion is essential because it plays a crucially important role in biological activity. The authors, both of whom are well known for their work in this field, describe in detail the major theoretical methods that are likely to be useful in the computer-aided design of drugs, enzymes and other molecules. A variety of theoretical and experimental studies is described and these are critically analyzed to provide a comprehensive picture of dynamic aspects of biomolecular structure and function. The book will be of interest to graduate students and research workers in structural biochemistry (X-ray diffraction and NMR), theoretical chemistry (liquids and polymers), biophysics, enzymology, molecular biology, pharmaceutical chemistry, genetic engineering and biotechnology.

Nuclear Magnetic Resonance (NMR) spectroscopy is the most powerful technique for characterization of biomolecular structures at atomic resolution in the solution state. This timely book, entitled "Biomolecular NMR Spectroscopy," focuses on the latest state-of-the-art NMR techniques for characterization of biological macromolecules in the solid and solution state. The editors, Dr. Andrew Dingley (University of Auckland, New Zealand) and Dr. Steven Pascal (Massey University, New Zealand) have organized the book into four sections, covering the following topics: sample preparation, structure and dynamics of proteins, structure and dynamics of nucleic acids and protein-nucleic acid complexes, and rapid and hybrid techniques--

Volume 17 is the second in a special topic series devoted to modern techniques in protein NMR, under the Biological Magnetic Resonance series. Volume 16, with the subtitle Modern Techniques in Protein NMR , is the first in this series. These two volumes present some of the recent, significant advances in the biomolecular NMR field with emphasis on developments during the last five years. We are honored to have brought together in these volume some of the world s foremost experts who have provided broad leadership in advancing this field. Volume 16 contains - vances in two broad categories: I. Large Proteins, Complexes, and Membrane Proteins and II. Pulse Methods. Volume 17 contains major advances in: I. Com- tational Methods and II. Structure and Dynamics. The opening chapter of volume 17 starts with a consideration of some important aspects of modeling from spectroscopic and diffraction data by Wilfred van Gunsteren and his colleagues. The next two chapters deal with combined automated assignments and protein structure determination, an area of intense research in many laboratories since the traditional manual methods are often inadequate or laborious in handling large volumes of NMR data on large proteins. First, Werner Braun and his associates describe their experience with the NOAH/DIAMOD protocol developed in their laboratory.