Published September 28, 1989
by Academic Press .
Written in English
|Contributions||John N. Abelson (Editor), Melvin I. Simon (Editor), Norman J. Oppenheimer (Editor), Thomas L. James (Editor)|
|The Physical Object|
|Number of Pages||530|
: Nuclear Magnetic Resonance Relaxation in Determination of Residue-Specific 15N Chemical Shift Tensors in Proteins in Solution: Protein Dynamics, Structure, and Applications of Transverse Relaxation Optimized Spectroscopy. Introduction; Analytical Approaches to Chemical Shift Determination from Relaxation Measurements. Purchase Nuclear Magnetic Resonance, Part B, Volume - 1st Edition. Print Book & E-Book. ISBN , Spin dynamics: basics of nuclear magnetic resonance Malcolm H. Levitt Spin Dynamics: Basics of Nuclear Magnetic Resonance, Second Edition is a comprehensive and modern introduction which focuses on those essential principles and concepts needed for a thorough understanding of the subject, rather than the practical aspects. Spin Dynamics: Basics of Nuclear Magnetic Resonance (2nd edition) Malcolm H. Levitt Spin Dynamics: Basics of Nuclear Magnetic Resonance, Second Edition is a comprehensive and modern introduction which focuses on those essential principles and concepts needed for a thorough understanding of the subject, rather than the practical aspects.
Nuclear magnetic resonance (NMR) spectroscopy is based on measuring the intensity of electromagnetic radiation absorbed by active atomic nuclei in the radiofrequency region. It is considered as a powerful analytical tool used by food scientists for examining the molecular structures of developed edible matrices. Nuclear magnetic resonance is one of the important mechanisms for determining their structures tures and properties. This book covers NMR techniques used in studying liquid crystals and present up. Nuclear magnetic resonance techniques provide powerful tools for investigating the elementary properties of quantum solids and fluids at very low : N.S. Sullivan. Molecular Dynamics Simulation Techniques f o r Determination o f Molecular S t r u c t u r e s from Nuclear Magnetic Resonance Data By R. M. SCHEEK, W. F. VAN GUNSTEREN, and R. KAPTEIN Introduction With the introduction of two-dimensional NMR techniques, ~ nuclear Overhauser enhancements (NOEs) became measurable for many proton pairs in a Cited by:
Good morning. NMR is not Nuclear Magnetic Spectroscopy, but "Nuclear Magnetic Ressonance". So, it's principle of working is neither emission or absorption. It's principle of working is subjecting the sample to a strong magnetic field, which allows certain atoms, called "paramagnetic atoms". Book Description. Nuclear magnetic resonance (NMR) is widely used across many fields of science because of the rich data it produces, and some of the most valuable data come from studies of nuclear spin relaxation in solution. The first edition of this book, published more than a decade ago, provided an accessible and cohesive treatment of the. The nuclear magnetic resonance (NMR) technique applied to biological systems is a powerful tool for structural determination and dynamics of both small organic molecules and biopolymers. The dynamic aspects and inherent flexibility play a central role in the facets of biological functionality [1,2]. Abstract. 1 H nuclear magnetic resonance (NMR) has proven to be a uniquely powerful tool for studying the structure of peptides in solution. I will concentrate on the type of structural information that is obtainable from NMR, the types of spectra needed to get this information, and how to interpret these by: 2.