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G Protein-Coupled Receptors
eBook Publisher: John Wiley & Sons
Imprint: Wiley
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G-Protein Coupled Receptors (GPCRs) are not only the largest protein family in the human genome but are also the single biggest target for therapeutic agents. Research into GPCRs is therefore growing at a fast pace and the range of techniques that can be applied to GPCRs is vast and continues to grow. This book provides an invaluable bench-side guide into the best and most up-to-date techniques for current and future research on GPCRs.
With contributions from leading international authorities, this book equips readers with clear and detailed protocols for both well-known and up-and-coming techniques along with hints and tips for success. All the methods have been tried and tested by leading international research labs and are presented in easy-to-follow stages along with a useful overview of each technique.
This book is an essential resource for all researchers in molecular biology, biochemistry, pharmacology and for graduate students.
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| Title of eBook: G Protein-Coupled Receptors | |
| Release Date: 12-11-2009 | |
| Publisher: Wiley |
This eBook download is available in the following formats:
| Parent title | G Protein-Coupled Receptors |
|---|---|
| Encrypted (DRM) | Yes |
| SKU | 9780470749227 |
| File size | 3535 |
| Security | n/a |
| Printing | Not allowed |
| Copying | Not allowed |
| Read aloud | No Sys requirements Download reader |
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| Note | Excellent navigation features are available via Adobe such as bookmarks and a quick access table of contents. Text search is easily accessible. An Adobe DRM-protected file is different than a pdf file in that it uses Adobe DRM (Digital Rights Management) technology, which authors and publishers use to protect their content from illegal online distribution and to set certain privileges such as restrictions on copying and printing. |
G Protein-Coupled Receptors
Chapter One
Measurement of Ligand-G Protein-coupled Receptor InteractionsKatie Leach, Celine Valant, Patrick M. Sexton and Arthur Christopoulos
Drug Discovery Biology Laboratory, Monash Institute of Pharmaceutical Sciences and Department of Pharmacology, Monash University, Parkville, 3052, Australia
1.1 Introduction
1.1.1 Ligand-receptor interactions and the law of mass action
Radioligand binding assays take advantage of the ability to detect the decay of radioactive material, which can be incorporated into a ligand of choice. The interaction of such a radioligand with a receptor preparation can subsequently be determined by capturing and measuring the amount of radioactivity present. Radioligand binding assays can be used to estimate molecular parameters, such as the density of receptors present in a tissue or cellular preparation or the affinity of a ligand for binding to a receptor.
The simplest scheme that describes the binding of a ligand to its receptor is based on the law of mass action:
[MATHEMATICAL EXPRESSION NOT REPRODUCIBLE IN ASCII]
where the ligand A binds to the receptor R to form the ligand-receptor complex AR. The rate at which the ligand binds to the receptor, expressed as the number of binding events per unit of time, is dependent on the ligand concentration, the number of unoccupied receptors and the association rate constant Kon. In contrast to an enzymatic reaction, there is no degradation of the product AR; and if this reaction is reversible, then the ligand-receptor complexes can dissociate into free receptor and ligand, which is dependent on the concentration of ligand
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