Protein Nmr Spectroscopy Practical Techniques And Applications Pdf
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One of the main drawbacks is lower sensitivity. In an atom with an odd mass number, the proton nucleus spins on its own axis.
NMR spectroscopy has proven to be a powerful technique to study the structure and dynamics of biological macromolecules. Beginning with elementary quantum mechanics, a set of practical rules is presented and used to describe many commonly employed multi-dimensional, multi-nuclear NMR pulse sequences.
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Skip to search form Skip to main content You are currently offline. Some features of the site may not work correctly. DOI: Nuclear Magnetic Resonance NMR spectroscopy, a physical phenomenon based upon the magnetic properties of certain atomic nuclei, has found a wide range of applications in life sciences over recent decades. The dramatic advances in NMR techniques have led to corresponding advances in the ability of NMR to study the structure, dynamics and interactions of biological macromolecules in solution under close to physiological conditions.
Overview DOI: Ligand protons that are in close contact with the receptor protein receive a higher degree of saturation, and as a result stronger STD NMR signals can be observed. Therefore, the STD NMR method is an excellent tool to investigate how a binding ligand interacts with its receptor molecule. This chapter comprises a detailed experimental protocol to acquire STD NMR spectra and determine the binding epitope of a ligand bound to its target protein. Antibody Data Search Beta.
Fundamentals of Protein NMR Spectroscopy
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application of nmr spectroscopy pdf
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