Pattern-Oriented Software Architecture Volume 3: Patterns for Resource Management by Michael Kircher, Prashant Jain

Download a book to kindle Pattern-Oriented Software Architecture Volume 3: Patterns for Resource Management by Michael Kircher, Prashant Jain 9780470845257

Download Pattern-Oriented Software Architecture Volume 3: Patterns for Resource Management PDF

Pattern-Oriented Software Architecture Volume 3: Patterns for Resource Management
Michael Kircher, Prashant Jain
Page: 266
Format: pdf, ePub, mobi, fb2
ISBN: 9780470845257
Publisher: Wiley

Download Pattern-Oriented Software Architecture Volume 3: Patterns for Resource Management

Download a book to kindle Pattern-Oriented Software Architecture Volume 3: Patterns for Resource Management by Michael Kircher, Prashant Jain 9780470845257

Overview

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.

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