Luminescence spectroscopy and circular dichroism
Author(s)
Bibliographic Information
Luminescence spectroscopy and circular dichroism
（Molecular anatomy and physiology of proteins series, . Methods in protein structure and stability analysis ; pt. A）（Nova biomedical）
Nova Science Publishers, c2007
Available at 2 libraries
Note
Includes bibliographical references and index
Description and Table of Contents
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 book gathers new leading-edge research from throughout the world in this exciting and exploding field of research.
Table of Contents
- Preface
- Introduction
- Multiparametric Approach in Analysis of Protein Structure and Unfolding-refolding Reaction
- Luminescence Spectroscopy
- Intrinsic Fluorescence in Protein Structure Analysis
- Analysis of Folded, Partially Folded and Misfolded Proteins with Fluorescent Dyes
- Time-resolved Fluorescence Energy Transfer
- Steady-state Quenching of Fluorescence to Study Protein Structure and Dynamics
- Local Dynamics of Macromolecules by Time-resolved Fluorescence Anisotropy
- Tryptophan Phosphorescence
- Time Resolved Protein Fluorescence in Multi-tryptophan Proteins
- Studies of Metal Binding Proteins by Intrinsic Luminescence Method
- Circular Dichroism
- Aromatic Side-chain Contributions to Protein Circular Dichroism
- Time-resolved Circular Dichroism as a Structural Probe of Rhodopsin Photolysis Intermediates
- Index.
by "Nielsen BookData"