Protein Ligand Interactions Structure And Spectroscopy PDF Download
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Author | : Stephen E. Harding |
Publisher | : Oxford University Press, USA |
Total Pages | : 474 |
Release | : 2001 |
Genre | : Medical |
ISBN | : 9780199637478 |
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This text on protein-ligand interactions offers a selection of the most useful and easily applied methods and acts as a guide to the principal techniques used.
Author | : G. Ulrich Nienhaus |
Publisher | : Humana Press |
Total Pages | : 568 |
Release | : 2005-03-21 |
Genre | : Science |
ISBN | : 9781588293725 |
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A readily reproducible collection of established and emerging techniques for studying the interaction between proteins and ligands, including biochemical/bulk techniques, structure analysis, spectroscopy, single-molecule studies, and theoretical/computational tools. Among the highlights are surface plasmon resonance (SPR) and reflectometric biosensor approaches, high-throughput screening with confocal optics microscopy, single molecule fluorescence and fluorescence correlation spectroscopy (FCS), atomic force microscopy (AFM), crystallography of reaction intermediates, and time-resolved x-ray crystallography. The protocols follow the successful Methods in Molecular BiologyTM series format, each offering step-by-step laboratory instructions, an introduction outlining the principle behind the technique, lists of the necessary equipment and reagents, and tips on troubleshooting and avoiding known pitfalls.
Author | : Stephen E. Harding |
Publisher | : |
Total Pages | : |
Release | : 2001 |
Genre | : Ligands (Biochemistry) |
ISBN | : |
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Author | : G. Ulrich Nienhaus |
Publisher | : Humana |
Total Pages | : 0 |
Release | : 2010-11-19 |
Genre | : Science |
ISBN | : 9781617375255 |
Download Protein'Ligand Interactions Book in PDF, ePub and Kindle
A readily reproducible collection of established and emerging techniques for studying the interaction between proteins and ligands, including biochemical/bulk techniques, structure analysis, spectroscopy, single-molecule studies, and theoretical/computational tools. Among the highlights are surface plasmon resonance (SPR) and reflectometric biosensor approaches, high-throughput screening with confocal optics microscopy, single molecule fluorescence and fluorescence correlation spectroscopy (FCS), atomic force microscopy (AFM), crystallography of reaction intermediates, and time-resolved x-ray crystallography. The protocols follow the successful Methods in Molecular BiologyTM series format, each offering step-by-step laboratory instructions, an introduction outlining the principle behind the technique, lists of the necessary equipment and reagents, and tips on troubleshooting and avoiding known pitfalls.
Author | : Hans-Joachim Böhm |
Publisher | : John Wiley & Sons |
Total Pages | : 262 |
Release | : 2006-03-06 |
Genre | : Science |
ISBN | : 3527605517 |
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The lock-and-key principle formulated by Emil Fischer as early as the end of the 19th century has still not lost any of its significance for the life sciences. The basic aspects of ligand-protein interaction may be summarized under the term 'molecular recognition' and concern the specificity as well as stability of ligand binding. Molecular recognition is thus a central topic in the development of active substances, since stability and specificity determine whether a substance can be used as a drug. Nowadays, computer-aided prediction and intelligent molecular design make a large contribution to the constant search for, e. g., improved enzyme inhibitors, and new concepts such as that of pharmacophores are being developed. An up-to-date presentation of an eternally young topic, this book is an indispensable information source for chemists, biochemists and pharmacologists dealing with the binding of ligands to proteins.
Author | : Holger Gohlke |
Publisher | : John Wiley & Sons |
Total Pages | : 361 |
Release | : 2012-05-21 |
Genre | : Medical |
ISBN | : 3527329668 |
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Innovative and forward-looking, this volume focuses on recent achievements in this rapidly progressing field and looks at future potential for development. The first part provides a basic understanding of the factors governing protein-ligand interactions, followed by a comparison of key experimental methods (calorimetry, surface plasmon resonance, NMR) used in generating interaction data. The second half of the book is devoted to insilico methods of modeling and predicting molecular recognition and binding, ranging from first principles-based to approximate ones. Here, as elsewhere in the book, emphasis is placed on novel approaches and recent improvements to established methods. The final part looks at unresolved challenges, and the strategies to address them. With the content relevant for all drug classes and therapeutic fields, this is an inspiring and often-consulted guide to the complexity of protein-ligand interaction modeling and analysis for both novices and experts.
Author | : Mark A. Williams |
Publisher | : Humana |
Total Pages | : 0 |
Release | : 2016-11-17 |
Genre | : Science |
ISBN | : 9781493958733 |
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Proteins are the cell’s workers, their messengers and overseers. In these roles, proteins specifically bind small molecules, nucleic acid and other protein partners. Cellular systems are closely regulated and biologically significant changes in populations of particular protein complexes correspond to very small variations of their thermodynamics or kinetics of reaction. Interfering with the interactions of proteins is the dominant strategy in the development of new pharmaceuticals. Protein Ligand Interactions: Methods and Applications, Second Edition provides a complete introduction to common and emerging procedures for characterizing the interactions of individual proteins. From the initial discovery of natural substrates or potential drug leads, to the detailed quantitative understanding of the mechanism of interaction, all stages of the research process are covered with a focus on those techniques that are, or are anticipated to become, widely accessible and performable with mainstream commercial instrumentation. Written in the highly successful Methods in Molecular Biology series format, chapters contain introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and notes on troubleshooting and avoiding known pitfalls. Authoritative and accessible, Protein Ligand Interactions: Methods and Applications, Second Edition serves as an ideal guide for researchers new to the field of biophysical characterization of protein interactions – whether they are beginning graduate students or experts in allied areas of molecular cell biology, microbiology, pharmacology, medicinal chemistry or structural biology.
Author | : Donald Huddler |
Publisher | : John Wiley & Sons |
Total Pages | : 148 |
Release | : 2017-10-02 |
Genre | : Science |
ISBN | : 111909948X |
Download Applied Biophysics for Drug Discovery Book in PDF, ePub and Kindle
Applied Biophysics for Drug Discovery is a guide to new techniques and approaches to identifying and characterizing small molecules in early drug discovery. Biophysical methods are reasserting their utility in drug discovery and through a combination of the rise of fragment-based drug discovery and an increased focus on more nuanced characterisation of small molecule binding, these methods are playing an increasing role in discovery campaigns. This text emphasizes practical considerations for selecting and deploying core biophysical method, including but not limited to ITC, SPR, and both ligand-detected and protein-detected NMR. Topics covered include: • Design considerations in biophysical-based lead screening • Thermodynamic characterization of protein-compound interactions • Characterizing targets and screening reagents with HDX-MS • Microscale thermophoresis methods (MST) • Screening with Weak Affinity Chromatography • Methods to assess compound residence time • 1D-NMR methods for hit identification • Protein-based NMR methods for SAR development • Industry case studies integrating multiple biophysical methods This text is ideal for academic investigators and industry scientists planning hit characterization campaigns or designing and optimizing screening strategies.
Author | : Elwy Hassan Abdelkader Ali |
Publisher | : |
Total Pages | : 0 |
Release | : 2016 |
Genre | : |
ISBN | : |
Download Protein-Ligand Interactions by NMR and EPR Spectroscopy Book in PDF, ePub and Kindle
Pulse electron paramagnetic resonance (EPR) distance measurements using double electron-electron resonance (DEER) experiments have been established as a powerful tool in structural biology. DEER experiments have the ability to measure the distance between two paramagnetic centres in biological macromolecules in the range of about 2 to 8 nm. The paramagnetic centres are usually introduced into proteins by site-directed spin labelling (SDSL) of cysteine residues. This thesis is based on the use of new lanthanide binding tags (LBTs) for paramagnetic nuclear magnetic resonance (NMR) spectroscopy (reported in papers 2 and 5), DEER distance measurements (reported in papers 1 and 3) and time-resolved luminescence resonance energy transfer (LRET) experiments (reported in paper 4). In particular, use of two complementary techniques, DEER experiments and paramagnetic NMR spectroscopy, was investigated for the study of conformational changes of proteins as a result of protein-ligand interactions. Two proteins were studied, the E. coli aspartate/glutamate binding protein (DEBP) and human calmodulin (CaM). Both proteins have different ligand binding characteristics: DEBP binds to small organic molecules, while CaM binds to specific peptide sequences. DEBP is a periplasmic binding protein responsible for the transport of aspartic acid and glutamic acid across the cell membrane and widely used in the design of biosensors of glutamate. The protein is composed of two domains, which bind one amino acid molecule at the domain interface. As DEBP contains a disulfide bond, an alternative cysteine-independent approach for site-specific protein tagging was used, which involved the use of genetically encoded unnatural amino acids that were site-specifically incorporated into proteins using orthogonal amber-suppressor tRNA/aminoacyl-tRNA synthetase systems. p-azido-L-phenylalanine (AzF) residues were incorporated into DEBP at different positions and paramagnetic lanthanide tags were attached to AzF via Cu(I)-catalyzed click chemistry (papers 1 and 2). Multiple Gd3+-Gd3+ distances measured by DEER experiments were used to define the metal positions, subsequently allowing deltachi-tensor determinations from sparse sets of pseudocontact shifts (PCSs). Both the DEER data and PCSs were in agreement with the closed conformation observed in the crystal structure of the homologue from S. flexneri. On the other hand, the PCSs indicated that the transition to the substrate-free protein involves a movement of the two domains as rigid entities relative to each other. CaM is a two-domain protein that acts as an intermediate messenger protein and intracellular calcium sensor, which responds to changes in Ca2+ concentrations by large conformational changes that enable binding to a range of different proteins involved in signalling pathways. The conformational changes of CaM upon binding of the myristoylated alanine-rich C-kinase substrate (MARCKS) peptide were studied using DEER experiments and paramagnetic NMR. MARCKS was chosen due to its unique binding mode compared to other CaM-target peptide complexes. The DEER results indicated that the binding of MARCKS peptide to CaM does not lock CaM in a single conformation. Deviations between the crystal and solution structure of the complex were also evident in the measured PCS data, highlighting the conformational flexibility of CaM that allows CaM to bind to diverse target proteins.
Author | : Silvia Tardioli |
Publisher | : |
Total Pages | : 197 |
Release | : 2011 |
Genre | : |
ISBN | : |
Download Optical Methods for Structure Elucidation of Protein-ligand Interactions: Fluorescence and Ultraviolet Resonance Raman Spectroscopy Book in PDF, ePub and Kindle