Conformation Of Biological Molecules
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Conformation of Biological Molecules
Author: G. Govil
language: en
Publisher: Springer Science & Business Media
Release Date: 2012-12-06
The determination of the three-dimensional structure of a biological molecule is the starting point in the understanding of molecular mechanisms involved in its complex biochemical reactions. The molecular architecture of multimolecular systems such as membranes and chromosomes provides the key to the fascinating field of molecular biology. Stereochemical details of biological macromolecules and their interactions with pharmacological agents form the basis for drug design. Naturally, the study of the structure and function of biological molecules has aroused tremendous interest and investigations in this area are being carried out in a large number of laboratories. The techniques used for this purpose include both experimental methods (X-ray and neutron diffraction measurements, study of NMR, ESR, vibrational and electronic spectra, ORD, CD and dipole moment measurements, biochemical modifications etc. ) and the oretical methods (quantum mechanical and classical potential energy calculations, Monte Carlo simulations and molecular graphics). F or several years now, X-ray diffraction [1] has served as our only source of infor mation on the three-dimensional arrangements of atoms in biopolymers. Fiber-diffrac tion of DNA led to the proposal of the DNA double helix. Fibers of long~hain polymers show ordering in the direction of the fibre-axis but not in the transverse plane. Accurate estimates of the dimensions of helical structures can be made using techniques on the basis of which models of biopolymers can be constructed.
Dynamic Aspects of Conformation Changes in Biological Macromolecules
Author: C. Sadron
language: en
Publisher: Springer Science & Business Media
Release Date: 2012-12-06
On the day after the 1959 Cambridge Congress, during which the International Union of Pure and Applied Biophysics was founded, a biophysics section was formed within the Society of Physical Chemistry (Societe de Chimie Physique). Since then, three of the Society's annual meetings (the 11th, 17th, and 23rd) were devoted exclusively to the physico-chemical study of biological systems. The first of these was held in June 1961 at a hotel in Col de Voza, at the foot of an alpine glacier above Chamonix. The second, in May 1967, took place in the more learned setting of the venerable rooms of the National Museum of Natural History in Paris. The third - the one dealt with in the present volume - was recently held at Orleans-La Source in the newly built lecture theatres of the young University, which is near the great Institutes of the National Centre for Scientific Research (CNRS), on the Sologne plateau. These three stages are milestones of an evolution which characterises (at least schematically) the explosive evolution of biological physico-chemistry. The first colloquium, with the title 'Deoxyribonucleic Acid: Structure, Synthesis and Functions', actually marks the first contact of the physical chemist with one of the then most prestigious biological macromolecules, the structure of which had just been discovered, and in this way celebrated one of the first and most striking successes of molecular biology.
Protein Conformational Dynamics
This book discusses how biological molecules exert their function and regulate biological processes, with a clear focus on how conformational dynamics of proteins are critical in this respect. In the last decade, the advancements in computational biology, nuclear magnetic resonance including paramagnetic relaxation enhancement, and fluorescence-based ensemble/single-molecule techniques have shown that biological molecules (proteins, DNAs and RNAs) fluctuate under equilibrium conditions. The conformational and energetic spaces that these fluctuations explore likely contain active conformations that are critical for their function. More interestingly, these fluctuations can respond actively to external cues, which introduces layers of tight regulation on the biological processes that they dictate. A growing number of studies have suggested that conformational dynamics of proteins govern their role in regulating biological functions, examples of this regulation can be found in signal transduction, molecular recognition, apoptosis, protein / ion / other molecules translocation and gene expression. On the experimental side, the technical advances have offered deep insights into the conformational motions of a number of proteins. These studies greatly enrich our knowledge of the interplay between structure and function. On the theoretical side, novel approaches and detailed computational simulations have provided powerful tools in the study of enzyme catalysis, protein / drug design, protein / ion / other molecule translocation and protein folding/aggregation, to name but a few. This work contains detailed information, not only on the conformational motions of biological systems, but also on the potential governing forces of conformational dynamics (transient interactions, chemical and physical origins, thermodynamic properties). New developments in computational simulations will greatly enhance our understanding of how these molecules function in various biological events.