This collection of state-of-the-art research describes the most frequently used techniques for structural analysis of proteins. Chapters focus on the impressive progress that has been made in the development of these techniques and identify future trends and research needs. Papers feature several spectroscopic techniques-including fluorescence spectroscopy, circular dichroism, and infrared spectroscopy.
|Series:||Pharmaceutical Biotechnology (closed) Series , #7|
|Product dimensions:||6.10(w) x 9.25(h) x 0.03(d)|
Table of Contents
Application of Fluorescence Spectroscopy for Determining the Structure and Function of Proteins; W. Jiskoot, et al. Structural Information on Proteins from Circular Dichroism Spectroscopy: Possibilities and Limitations; M. Bloemendal, W.C. Johnson, Jr. Fourier Transform Infrared Spectroscopy Investigations of Protein Structure; E.A. Cooper, K. Knutson. Two, Three, and Four-dimensional Nuclear Magnetic Resonance (NMR) Spectroscopy of Protein Pharmaceuticals; D.G. Vander, Velde et al. Thermodynamic Strategies for Rational Protein and Drug Design; K.P. Murphy, E. Freire. Chromatographic Techniques for the Characterization of Proteins; J.J.M. Hothuis, R.J. Driebergen. Capillary Electrophoresis of Proteins; T.A.A.M. van de Goor. Applying Genetic Engineering to the Structural Analysis of Proteins; P.T. Hamilton. Index.