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Methods in Protein Structure and Stability Analysis: Luminescence Spectroscopy and Circular Dichroism
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Editors: Vladimir N. Uversky (Indiana University School of Medicine) and Eugene A. Permyakov (Russian Academy of Sciences)
Book Description:
Protein research is a frontier field in science. Proteins are widely distributed in plants and animals and are the principal constituents of the protoplasm of all cells, and consist essentially of combinations of a-amino acids in peptide linkages. Twenty different amino acids are commonly found in proteins, and serve as enzymes, structural elements, hormones, immunoglobulins, etc., and are involved throughout the body, and in photosynthesis. This new book gathers new leading-edge research from throughout the world in this exciting and exploding field of research.

Table of Contents:
Preface;

Section 1 - Introduction
Chapter 1.1 - Multiparametric approach in analysis of protein structure and unfolding-refolding reaction; pp. 3-52
(Uversky V.N.)

Section 2 - Luminescence Spectroscopy
Chapter 2.1- Intrinsic fluorescence in protein structure analysis; pp. 55-72
(Ross J.B., Laws W.R.)

Chapter 2.2 - Analysis of folded, partially folded and misfolded proteins with fluorescent dyes; pp. 73-104
(Kuznetsova I.M., Turoverov K.K., Dunker A.K., Uversky V.N.)

Chapter 2.3 - Time-resolved fluorescence energy transfer;
pp. 105-152
(Haas Elisia)

Chapter 2.4 - Steady-state quenching of fluorescence to study protein structure and dynamics; pp. 153-185
(Béla Somogyi, Miklós Nyitrai, Gábor Hild)

Chapter 2.5 - Local dynamics of macromolecules by time-resolved fluorescence anisotropy; pp. 187-199
(Ross J.B., Laws W.R.)

Chapter 2.6 - Tryptophan phosphorescence; pp. 201-236
(Permyakov E.A.)

Chapter 2.7 - Time resolved protein fluorescence in multi-tryptophan proteins; pp. 237-256
(Engelborghs Y., Hellings M.)

Chapter 2.8 - Studies of metal binding proteins by intrinsic luminescence method; pp. 257-287
(Permyakov E.A.)

Section 3 - Circular Dichroism

Chapter 3.1 - Aromatic side-chain contributions to protein circular dichroism; pp. 291-344
(Robert W. Woody)

Chapter 3.2 - Time-resolved circular dichroism as a structural probe of rhodopsin photolysis intermediates; pp. 345-356
(Lewis J.W., Gu-Thomas Y., Kliger D.)

Index

   Series:
      Molecular Anatomy and Physiology of Proteins - Vladimir N. Uversky (Indiana University of Medicine, USA), Series Editor
   Binding: Hardcover
   Pub. Date: 2007
   ISBN: 1-60021-404-5
   Status: AV
  
Status Code Description
AN Announcing
FM Formatting
PP Page Proofs
FP Final Production
EP Editorial Production
PR At Prepress
AP At Press
AV Available
  
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Methods in Protein Structure and Stability Analysis: Luminescence Spectroscopy and Circular Dichroism