Methods in Protein Structure & Stability Analysis

Texte du rabat

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.

Résumé
Protein research is a frontier field in science. Proteins are 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. This book gathers research from throughout the world in this field of research.

Contenu
Preface; NMR and EPR Spectroscopy; Analysing Protein Folding by NMR; EPR Methods for Evaluating Copper Binding Sites in Prion and other Partially Structured Proteins; Variable Velocity Liquid Flow EPR and Submillisecond Protein Folding; EPR/ESR/EMR Methods for Studying Calcium Binding Proteins; Mass-Spectrometry; Stopped-flow Electrospray Ionisation Mass Spectrometry; Modern Mass Spectrometry and Proteomic Methods Applied to Biomarker Identification and Drug Target Discovery; Analysis of Partially Folded Proteins by Electron Ionisation Mass Spectrometry; Protein Imaging; Atomic Force Microscopy; Protein Structure by Cryo-electron Microscopy; Miscellaneous; Time-resolved Optical Rotatory Dispersion Studies of Azobenzene Cross-Linked Peptides; Phase Diagram Method for Analysis of Protein Folding; The use of Protein Engineering Methods for Studies of Calcium Binding Proteins; Analysis of Membrane-bound Protein Association using Fluorescence Spectroscopy; The Role of Aromatic Interactions in Folding, Stability and Molecular Recognition of Proteins and Polypeptides; Index.