Download or read book Protein Dynamics Loop Motions and Protein protein Interactions Combining Nuclear Magnetic Resonance nmr Spectroscopy with Molecular Dynamics md Simulations written by Yina Gu and published by . This book was released on 2016 with total page 196 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Biological NMR Spectroscopy written by John L. Markley and published by Oxford University Press. This book was released on 1997-01-30 with total page 375 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book presents a critical assessment of progress on the use of nuclear magnetic resonance spectroscopy to determine the structure of proteins, including brief reviews of the history of the field along with coverage of current clinical and in vivo applications. The book, in honor of Oleg Jardetsky, one of the pioneers of the field, is edited by two of the most highly respected investigators using NMR, and features contributions by most of the leading workers in the field. It will be valued as a landmark publication that presents the state-of-the-art perspectives regarding one of today's most important technologies.
Download or read book Structure Computation and Dynamics in Protein NMR written by N. Rama Krishna and published by Springer Science & Business Media. This book was released on 2006-05-09 with total page 565 pages. Available in PDF, EPUB and Kindle. Book excerpt: 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.
Download or read book Practical Medicinal Chemistry with Macrocycles written by Eric Marsault and published by John Wiley & Sons. This book was released on 2017-09-12 with total page 617 pages. Available in PDF, EPUB and Kindle. Book excerpt: Including case studies of macrocyclic marketed drugs and macrocycles in drug development, this book helps medicinal chemists deal with the synthetic and conceptual challenges of macrocycles in drug discovery efforts. Provides needed background to build a program in macrocycle drug discovery –design criteria, macrocycle profiles, applications, and limitations Features chapters contributed from leading international figures involved in macrocyclic drug discovery efforts Covers design criteria, typical profile of current macrocycles, applications, and limitations
Download or read book NMR of Proteins written by Clore and published by CRC Press. This book was released on 1993 with total page 328 pages. Available in PDF, EPUB and Kindle. Book excerpt: Determination of structures of larger proteins in solution by three- and four-dimensional heteronuclear magnetic resonance spectroscopy. Methodological advances in protein NMR. Determination of high-resolution NMR structures of proteins. Multidimensional NMR studies of immunosuppressant/immunophilin complexes. NMR studies of the structure and role of modules involved in protein-protein interactions. NMR structural studies of membrane proteins. Heteronuclear NMR studies of the molecular synamics of staphylococcal nuclease. Study of protein dynamics by NMR. The folding, stability and dynamics of T4 lysozyme: a perspective using nuclear magnetic resonance.
Download or read book Predictions of Protein Chemical Shifts and Protein Slow Motions written by Sishi Tang and published by . This book was released on 2011 with total page 205 pages. Available in PDF, EPUB and Kindle. Book excerpt: Nuclear magnetic resonance spectroscopy (NMR) is one of the most powerful biophysical techniques for studying biomacromolecules. The advances of NMR techniques are often facilitated by the development of computational methods for the purpose of data interpretation and analyses. In this way, more information is extracted from the experimental measurements and complementary descriptions are given to details elusive to NMR probes, so that the structural and dynamical behavior of the biomolecule can be adequately described. Hence the two major goals of this thesis are: i) To calculate chemical shift anisotropy (CSA) accurately and to understand how CSA is influenced by the local environment. ii) To predict and characterize important metastable conformations of proteins probed in NMR relaxation experiments. The first aspect is covered by three chapters (Chapter 2 - 4), where CSA calculations using QM and QM/MM models are described and compared. First, we used a small fragment (NMA3) model to determine the effect of vibrational motion on the magnitude and orientation of CSAs. Next, we applied the same model to predict chemical shift tensors and achieve qualitative agreement with experimental measurements for the GB1 protein. Later we showed that a more expanded AF-QM/MM (automated ii fragment quantum mechanical/molecular mechanical) model is able to provide better quantitative predictions to chemical shift tensors via an appropriate representation of environmental effects. Our study is expected to compensate for the lack of direct experimental measurements of CSAs, and help uncover the rich structural information hidden in CSA data. The second aspect is covered by four chapters (Chapter 5 - 8), where we used the loop motion of triosephosphate isomerase (TIM) as our primary model to study protein conformational changes. To corroborate the "population shift" theory, conventional MD simulations was first performed to show that metastable states of TIM can be induced and stabilized. Then adaptively biased molecular dynamics (ABMD) simulations were used to predict and characterize the metastable conformations for monomeric TIM. In order to characterize the free energy landscape of this loop motion accurately and efficiently, an iterative approach combining ABMD and umbrella sampling was developed. Subsequently, this approach was applied to understand why TIM is only active as a dimer from energy and dynamics perspectives. Futhermore, we extended the ABMD method so that the metastable states of proteins can be predicted from their essential motions. The details of the methods used to predict and characterize protein minor conformations are described, providing insights into the energy and dynamics programmed in protein functions.
Download or read book Allostery written by Aron W. Fenton and published by Humana Press. This book was released on 2011-11-04 with total page 0 pages. Available in PDF, EPUB and Kindle. Book excerpt: Despite considerable variability within the scientific community, allosteric regulation can best be defined functionally as how a macromolecule binds one ligand differently when a second ligand is or is not pre-bound to the macromolecule, which constitutes a vital aspect of protein structure/function. In Allostery: Methods and Protocols, expert researchers in the field provide key techniques to investigate this biological phenomenon. Focusing on heterotropic systems with some coverage of homotropic systems, this volume covers the monitoring of allosteric function, allosteric conformational changes, and allosteric changes in protein dynamics/sub-population distribution, as well as topics such as macromolecular and ligand engineering of allosteric functions and computational aids in the study of allostery. Written in the highly successful Methods in Molecular BiologyTM series format, the chapters include the kind of detailed description and implementation advice that is crucial for getting optimal results in the laboratory. Thorough and intuitive, Allostery: Methods and Protocols aids scientists in continuing to study ligand-induced, through-protein effects on protein function (ligand binding/catalysis), a phenomenon that is well recognized through the history of the life sciences and very poorly understood at the molecular level.
Download or read book Improved Methods for Characterization of Protein Dynamics by NMR spectroscopy and Studies of the EphB2 Kinase Domain written by Alexandra Ahlner and published by Linköping University Electronic Press. This book was released on 2015-04-15 with total page 79 pages. Available in PDF, EPUB and Kindle. Book excerpt: Proteins are essential for all known forms of life and in many lethal diseases protein failure is the cause of the disease. To understand proteins and the processes they are involved in, it is valuable to know their structures as well as their dynamics and interactions. The structures may not be directly inspected because proteins are too small to be visible in a light microscope, which is why indirect methods such as nuclear magnetic resonance (NMR) spectroscopy have to be utilized. This method provides atomic information about the protein and, in contrast to other methods with similar resolution, the measurements are performed in solution resulting in more physiological conditions, enabling analysis of dynamics. Important dynamical processes are the ones on the millisecond timeframe, which may contribute to interactions of proteins and their catalysis of chemical reactions, both of significant value for the function of the proteins. To better understand proteins, not only do we need to study them, but also develop the methods we are using. This thesis presents four papers about improved NMR techniques as well as a fifth where the kinase domain of ephrinB receptor 2 (EphB2) has been studied regarding the importance of millisecond dynamics and interactions for the activation process. The first paper presents the software COMPASS, which combines statistics and the calculation power of a computer with the flexibility and experience of the user to facilitate and speed up the process of assigning NMR signals to the atoms in the protein. The computer program PINT has been developed for easier and faster evaluation of NMR experiments, such as those that evaluate protein dynamics. It is especially helpful for NMR signals that are difficult to distinguish, so called overlapped peaks, and the soft- ware also converts the detected signals to the indirectly measured physical quantities, such as relaxation rate constants, principal for dynamics. Next are two new versions of the Carr-Purcell-Maiboom-Gill (CPMG) dispersion pulse sequences, designed to measure millisecond dynamics in a way so that the signals are more separated than in standard experiments, to reduce problems with overlaps. To speed up the collection time of the data set, a subset is collected and the entire data set is then reconstructed, by multi-dimensional decomposition co-processing. Described in the thesis is also a way to produce suitably labeled proteins, to detect millisecond dynamics at C? positions in proteins, using the CPMG dispersion relaxation experiment at lower protein concentrations. Lastly, the kinase domain of EphB2 is shown to be more dynamic on the millisecond time scale as well as more prone to interact with itself in the active form than in the inactive one. This is important for the receptor function of the protein, when and how it mediates signals. To conclude, this work has extended the possibilities to study protein dynamics by NMR spectroscopy and contributed to increased understanding of the activation process of EphB2 and its signaling mechanism.
Download or read book Collective Langevin dynamics of conformational motions in proteins written by Oliver Lange and published by Cuvillier Verlag. This book was released on 2006 with total page 16 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Comparative Studies of Protein Structure and Dynamics by Molecular Dynamics Simulation NMR Spectroscopy and X ray Crystallography written by and published by . This book was released on 1999 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book The Critical Assessment of Protein Dynamics Using Molecular Dynamics MD Simulations and Nuclear Magnetic Resonance NMR Spectroscopy Experimentation written by Andrew Hsu and published by . This book was released on 2020 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: We derive the inverse Gaussian probability distribution function from general properties of spectral density functions at low and high frequencies for macromolecules in solution, using the principle of maximum entropy. The resulting model-free spectral density functions are finite at a frequency of zero and can be used to describe distributions of either overall or internal correlation times using the model-free ansatz. The approach is validated using 15N backbone relaxation data for the intrinsically disordered, DNA-binding region of the bZip transcription factor domain of the Saccharomyces cerevisiae protein GCN4, in the absence of cognate DNA.
Download or read book Protein Dynamics Using NMR Relaxation written by Kevin H. Mayo and published by . This book was released on 2006-01-01 with total page 300 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book specifically addresses the use of (13)C and (15)N NMR spectroscopy to derive information on the internal motions of proteins and peptides in solution. Basic methods of NMR relaxation, along with the general theory of correlation functions and spectral densities, are first covered, followed by in-depth analyses and comparisons of various motional models and molecular dynamics simulations used to derive protein dynamics information from NMR relaxation experiments. Motional model equations are expressed in computer program-ready format. The text is ideally suited for graduate and post-graduate students as well as experienced professionals.
Download or read book Protein NMR written by Lawrence Berliner and published by Springer. This book was released on 2015-08-24 with total page 193 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book covers new techniques in protein NMR, from basic principles to state-of-the-art research. It covers a spectrum of topics ranging from a “toolbox” for how sequence-specific resonance assignments can be obtained using a suite of 2D and 3D NMR experiments and tips on how overlap problems can be overcome. Further topics include the novel applications of Overhauser dynamic nuclear polarization methods (DNP), assessing protein structure, and aspects of solid-state NMR of macroscopically aligned membrane proteins. This book is an ideal resource for students and researchers in the fields of biochemistry, chemistry, and pharmacology and NMR physics. Comprehensive and intuitively structured, this book examines protein NMR and new novel applications that include the latest technological advances. This book also has the features of: • A selection of various applications and cutting-edge advances, such as novel applications of Overhauser dynamic nuclear polarization methods (DNP) and a suite of 2D and 3D NMR experiments and tips on how overlap problems can be overcome • A pedagogical approach to the methodology • Engaging the reader and student with a clear, yet critical presentation of the applications
Download or read book Collective Langevin Dynamics of Conformational Motions in Protein written by and published by Cuvillier Verlag. This book was released on 2006-01-06 with total page 164 pages. Available in PDF, EPUB and Kindle. Book excerpt:
Download or read book Solid State NMR Spectroscopy written by Melinda J. Duer and published by John Wiley & Sons. This book was released on 2008-04-15 with total page 592 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book is for those familiar with solution-state NMR who are encountering solid-state NMR for the first time. It presents the current understanding and applications of solid-state NMR with a rigorous but readable approach, making it easy for someone who merely wishes to gain an overall impression of the subject without details. This dual requirement is met through careful construction of the material within each chapter. The book is divided into two parts: "Fundamentals" and "Further Applications." The section on Fundamentals contains relatively long chapters that deal with the basic theory and practice of solid-state NMR. The essential differences and extra scope of solid-state NMR over solution-state is dealt with in an introductory chapter. The basic techniques that all chapters rely on are collected into a second chapter to avoid unnecessary repetition later. Remaining chapters in the "Fundamentals" part deal with the major areas of solid-state NMR which all solid-state NMR spectroscopists should know about. Each begins with an overview of the topic that puts the chapter in context. The basic principles upon which the techniques in the chapter rely are explained in a separate section. Each of these chapters exemplifies the principles and techniques with the applications most commonly found in current practice. The "Further Applications" section contains a series of shorter chapters which describe the NMR techniques used in other, more specific areas. The basic principles upon which these techniques rely will be expounded only if not already in the Fundamentals part.
Download or read book Protein NMR for the Millennium written by N. Rama Krishna and published by Springer Science & Business Media. This book was released on 2006-04-11 with total page 345 pages. Available in PDF, EPUB and Kindle. Book excerpt: Protein NMR for the Millennium is the third volume in a special thematic series devoted to the latest developments in protein NMR under the Biological Magnetic Resonance umbrella. This book is divided into three major sections dealing with significant recent advances in the study of large proteins in solution and solid state, structure refinement, and screening of bioactive ligands. Key Features: TROSY, Segmental isotope labeling of proteins, Hydrogen bond scalar couplings, Structure refinement based on residual dipolar couplings, Written by the world's foremost experts who have provided broad leadership in advancing the protein NMR field.
Download or read book Experimental Approaches of NMR Spectroscopy written by The Nuclear Magnetic Resonance Society of Japan and published by Springer. This book was released on 2017-11-23 with total page 634 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book describes the advanced developments in methodology and applications of NMR spectroscopy to life science and materials science. Experts who are leaders in the development of new methods and applications of life and material sciences have contributed an exciting range of topics that cover recent advances in structural determination of biological and material molecules, dynamic aspects of biological and material molecules, and development of novel NMR techniques, including resolution and sensitivity enhancement. First, this book particularly emphasizes the experimental details for new researchers to use NMR spectroscopy and pick up the potentials of NMR spectroscopy. Second, the book is designed for those who are involved in either developing the technique or expanding the NMR application fields by applying them to specific samples. Third, the Nuclear Magnetic Resonance Society of Japan has organized this book not only for NMR members of Japan but also for readers worldwide who are interested in using NMR spectroscopy extensively.
