Analysis Of Ribose Dynamics In Rna Molecules Utilizing 13c Nmr Spin Relaxation Techniques Determined With Novel Specific Isotope Labeling Scheme

This volume, written by experts in the field, discusses the current understanding of the biophysical principles that govern RNA folding, with featured RNAs including the ribosomal RNAs, viral RNAs, and self-splicing introns. In addition to the fundamental features of RNA folding, the central experimental and computational approaches in the field are presented with an emphasis on their individual strengths and limitations, and how they can be combined to be more powerful than any method alone; these approaches include NMR, single molecule fluorescence, site-directed spin labeling, structure mapping, comparative sequence analysis, graph theory, course-grained 3D modeling, and more. This volume will be of interest to professional researchers and advanced students entering the field of RNA folding.

The second edition of a highly acclaimed handbook and ready reference. Unmatched in its breadth and quality, around 100 specialists from all over the world share their up-to-date expertise and experiences, including hundreds of protocols, complete with explanations, and hitherto unpublished troubleshooting hints. They cover all modern techniques for the handling, analysis and modification of RNAs and their complexes with proteins. Throughout, they bear the practising bench scientist in mind, providing quick and reliable access to a plethora of solutions for practical questions of RNA research, ranging from simple to highly complex. This broad scope allows the treatment of specialized methods side by side with basic biochemical techniques, making the book a real treasure trove for every researcher experimenting with RNA.

Spin relaxation parameters, although difficult to interpret, are attracting interest in NMR as these parameters are capable of yielding both structural and dynamic information. Cross-relaxation and cross-correlation parameters afford a non-ambiguous approach to molecular structure and dynamics although they require some special skills for their experimental determination and for their exploitation. This work will start with an introduction to nuclear spin cross-relaxation and cross-correlation phenomena in liquids then look in more detail at molecules in soft matter and large biomolecules. Providing a detailed, timely account, the authors are filling a gap in the present NMR literature for the analytical scientist.

In this book, leading researchers in the field of Bioinformatics provide a selection of the most useful and widely applicable methods, able to be applied as is, or with minor variations, to many specific problems. Over 80 authors from around the globe contribute to the two volumes, including many leading experts in their respective subjects. They encompass topics from across the diverse field of bioinformatics through its broad scope, combining to provide an inter-disciplinary collaboration involving biologists, biochemists, physicists, mathematicians, statisticians and computer scientists.

NMR spectroscopy has undergone a revolution in recent years with the advent of several new methods overcoming the problems of sensitivity and resolution. Recent developments in biotechnology have made it easier and economical to introduce 13C, 15N and 2H into proteins and nucleic acids. At the same time, there has been an explosion in the number of NMR experiments that utilize such isotope labeled samples. Thus, a combination of isotopic labeling and multidimensional, multinuclear NMR has opened up new avenues for structural studies of proteins, nucleic acids and their complexes. This book will focus on recent developments in isotope labeling methods for structural studies of small molecules, peptides, proteins and nucleic acids. The aim of the book is to serve as a compendium of isotope labeling for the biomolecular NMR community providing comprehensive coverage of the existing methods and latest developments along with protocols and practical hints on the various experimental aspects. The book will cover a wide range of topics in isotope labeling under one title including emerging areas of metabolonomics and solid state NMR.

RNA is a structurally flexible and dynamic molecule, and rapidly interconverts between multiple conformations. Despite the significant advances in traditional biophysical techniques like NMR spectroscopy and X-ray crystallography it is difficult to resolve the structures of dynamically inter-converting states as these methods measure the average property of an ensemble of molecules. It is necessary to resolve and get detailed descriptions of the multiple conformational structures, their quantitative distribution and their related dynamics in order to understand the ruggedness of the energy landscape. The present study attempts to link the conformational dynamics of RNA to its structure and biological function. Ultrafast time-resolved fluorescence spectroscopy is used to probe the distribution of multiple conformations and their dynamics that occur on a very fast timescales. This tool uses the resolution of time domain behavior of 2-aminopurine fluorescence decay on the ultrafast timescale to capture the characteristics of different structures. The RNAs are labeled with the fluorescent base analog 2-aminopurine to probe the base stacking patterns in RNA. Base stacking interactions is a unique feature that defines nucleic acid structures compared to proteins and are the major stabilizing force in RNA. Chapter 1 discusses the RNA folding mechanism and the relationships between sequence, structure, dynamics and function and explains the advantage of using ultrafast time resolved spectroscopy in defining structure-function relationships in RNA. Chapter 2 discusses the conformational heterogeneity and dynamics in purine-sensing riboswitches. We observed multiple conformations where the ligand is significantly stacked with the bases of the binding pocket and shows a dynamic balance between base stacking interactions and hydrogen bonding to achieve specificity and high affinity by the aptamer domain. Chapter 3 explores the conformational heterogeneity of GAAA tetraloop receptor and the impacts of the tertiary interactions between the receptor and the GAAA tetraloop, where we probe the isolated and GAAA-tetraloop bound receptor. The presence of any bound conformation in the free receptor state leads us to propose the conformational capture mechanism in tetraloop-receptor recognition. Chapter 4 summarizes findings of employing the ultrafast spectroscopy approach in studying riboswitches and the GAAA tetraloop-receptor. Overall our research is an effort to understand the role of conformational dynamics in RNA folding, tertiary interactions, recognition and functions.

This textbook provides a unique and thorough look at the application of chemical biomarkers to aquatic ecosystems. Defining a chemical biomarker as a compound that can be linked to particular sources of organic matter identified in the sediment record, the book indicates that the application of these biomarkers for an understanding of aquatic ecosystems consists of a biogeochemical approach that has been quite successful but underused. This book offers a wide-ranging guide to the broad diversity of these chemical biomarkers, is the first to be structured around the compounds themselves, and examines them in a connected and comprehensive way. This timely book is appropriate for advanced undergraduate and graduate students seeking training in this area; researchers in biochemistry, organic geochemistry, and biogeochemistry; researchers working on aspects of organic cycling in aquatic ecosystems; and paleoceanographers, petroleum geologists, and ecologists. Provides a guide to the broad diversity of chemical biomarkers in aquatic environments The first textbook to be structured around the compounds themselves Describes the structure, biochemical synthesis, analysis, and reactivity of each class of biomarkers Offers a selection of relevant applications to aquatic systems, including lakes, rivers, estuaries, oceans, and paleoenvironments Demonstrates the utility of using organic molecules as tracers of processes occurring in aquatic ecosystems, both modern and ancient