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Solid State NMR Spectroscopy for Biopolymers: Principles and Applications
 
 

Solid State NMR Spectroscopy for Biopolymers: Principles and Applications [Kindle Edition]

Hazime Saitô , Isao Ando , Akira Naito

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Print List Price: $179.00
Kindle Price: $127.20 includes free wireless delivery via Amazon Whispernet
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Editorial Reviews

Review

From the reviews: "This book surveys much of the current research in the area of biological solid-state NMR spectroscopy, and as such should be of great interest to the chemical, biochemical, and biophysical communities. The level is appropriate for graduate students, and the book would be an excellent textbook for a graduate level course in biological solid-state NMR spectroscopy. Its publication is timely considering the recent numerous developments in this area … ." (Michele Auger, Journal of the American Chemical Society, Vol. 129 (10), 2007)

Product Description

When considering the biological significance and industrial and medical applications of biopolymers, it is crucial to know details of their secondary structure, dynamics and assembly. The biopolymers include globular, membrane and fibrous proteins, polypeptides, nucleic acids, polysaccharides and lipids. Solid state NMR spectroscopy has proved to be the most suitable and unrivaled means for investigations of biopolymers. The major advantage of solid state NMR spectroscopy is that the resulting line widths can be manipulated experimentally and are not influenced by motional fluctuation of proteins under consideration as a whole.


Solid State NMR Spectroscopy for Biopolymers: Principles and Applications provides a comprehensive account on how the conformation and dynamics of such biopolymers can be revealed by solid state NMR spectroscopy. Special efforts have been made towards the historical and chronological consequences of a variety of applications and the dynamic aspects of the biopolymer system. In particular, the authors emphasise how important it is to record the most simple DD-MAS (one pulse excitation with high power decoupling) as a means of locating very flexible portions of membrane proteins and membrane associated peptides. The authors also demonstrate that dynamic features of membrane proteins with a timescale of fast (108 Hz) and intermediate (104 -105 Hz) fluctuation motions can be revealed easily by specific suppression of peaks.


Product Details

  • Format: Kindle Edition
  • File Size: 7090 KB
  • Publisher: Springer; 1 edition (August 18, 2006)
  • Sold by: Amazon Digital Services
  • Language: English
  • ASIN: B00193HMNK
  • Text-to-Speech: Enabled
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