Annual Reports on NMR Spectroscopy
- 1st Edition, Volume 45 - November 23, 2001
- Latest edition
- Editor: Graham A. Webb
- Language: English
Nuclear magnetic resonance (NMR) is an analytical tool used by chemists and physicists to study the structure and dynamics of molecules. In recent years, no other technique has… Read more
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Description
Description
Nuclear magnetic resonance (NMR) is an analytical tool used by chemists and physicists to study the structure and dynamics of molecules. In recent years, no other technique has grown to such importance as NMR spectroscopy. It is used in all branches of science where precise structural determination is required and where the nature of interactions and reactions in solution is being studied.
Annual Reports on NMR Spectroscopy has established itself as a means for the specialist and nonspecialist alike to become familiar with new applications of NMR spectroscopy in all branches of chemistry.
As with other members of this series, Volume 45 consists of a collection of accounts of progress in various areas of NMR activity. The first report covers Temperature Measurements using NMR, following this is a review on Structural Studies of Amino Acids, Polypeptides and Proteins in the Solid State. The next contribution is on STRAFI and SPI Magnetic Resonance Imaging. The final contribution is a report on NMR Studies of Internal Hydrogen Bonds in Metalloproteins.
Annual Reports on NMR Spectroscopy has established itself as a means for the specialist and nonspecialist alike to become familiar with new applications of NMR spectroscopy in all branches of chemistry.
As with other members of this series, Volume 45 consists of a collection of accounts of progress in various areas of NMR activity. The first report covers Temperature Measurements using NMR, following this is a review on Structural Studies of Amino Acids, Polypeptides and Proteins in the Solid State. The next contribution is on STRAFI and SPI Magnetic Resonance Imaging. The final contribution is a report on NMR Studies of Internal Hydrogen Bonds in Metalloproteins.
Key features
Key features
- Temperature Measurements using NMR
- Structural Studies of Amino Acids, Polypeptides and Proteins, in the Solid State by 1H CRAMPS NMR
- Stray Field (STRAFI) and Single Point (SPI) Magnetic Resonance Imaging
- NMR Studies of Internal Hydrogen Bonds in Metalloproteins
- Structural Studies of Amino Acids, Polypeptides and Proteins, in the Solid State by 1H CRAMPS NMR
- Stray Field (STRAFI) and Single Point (SPI) Magnetic Resonance Imaging
- NMR Studies of Internal Hydrogen Bonds in Metalloproteins
Readership
Readership
Chemists, physicists, and materials scientists studying properties of solids and those using NMR spectroscopy.
Table of contents
Table of contents
- Temperature Measurements using NMR
- Structural Studies of Amino Acids, Polypeptides and Proteins, in the Solid State by 1H CRAMPS NMR
- Stray Field (STRAFI) and Single Point (SPI) Magnetic Resonance Imaging
- NMR Studies of Internal Hydrogen Bonds in Metalloproteins
- Structural Studies of Amino Acids, Polypeptides and Proteins, in the Solid State by 1H CRAMPS NMR
- Stray Field (STRAFI) and Single Point (SPI) Magnetic Resonance Imaging
- NMR Studies of Internal Hydrogen Bonds in Metalloproteins
Product details
Product details
- Edition: 1
- Latest edition
- Volume: 45
- Published: November 23, 2001
- Language: English
About the editor
About the editor
GW
Graham A. Webb
Editor of about 150 volumes, mostly dealing with aspects of NMR. Retired Professor of Chemistry from the University of Surrey.
Affiliations and expertise
Royal Society of Chemistry, Burlington House, London, UKView book on ScienceDirect
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