| Description |
1 online resource |
| Contents |
Intro -- Preface -- Contents -- About the Editors -- 1: Protein Purification, Estimation, Storage, and Effect on Structure-Function-Dynamics -- 1.1 Introduction -- 1.2 Protein Purification -- 1.2.1 Protein Precipitation/Salting Out -- 1.2.2 Buffer Exchange/Dialysis -- 1.2.3 Immuno-Affinity Chromatography -- 1.2.4 Affinity Chromatography -- 1.2.5 Ion-Exchange Chromatography -- 1.2.6 Size-Exclusion or Gel Filtration Chromatography (SEC/GFC) -- 1.2.7 High-Pressure/Performance Liquid Chromatography (HPLC) -- 1.2.8 Hydrophobic Interaction Chromatography -- 1.3 Resolving and Display of Protein |
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1.6.3 Cycles of Freeze-Thaw -- 1.6.4 Organic Solvents and pH -- 1.6.5 Proteases/Peptidases -- 1.6.6 Protein Concentration -- 1.6.7 Reducing Agents -- 1.6.8 Salt Conditions and Urea -- 1.6.9 Temperature -- 1.7 Factors Affecting the Stability of Proteins -- 1.8 Effect on the Dynamics of Protein -- 1.9 Conclusions -- References -- 2: Experimental and Computational Methods to Determine Protein Structure and Stability -- 2.1 Protein Purification Techniques -- 2.1.1 General Aspects of Protein Purification -- 2.1.2 Stabilizing Proteins -- 2.1.3 Quantification of Proteins |
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2.1.4 Purification of Proteins Based on Solubility -- 2.1.5 Purification of Proteins Based on Size -- 2.1.5.1 Ultrafiltration -- 2.1.5.2 Gel Filtration or Molecular Sieve or Size Exclusion Chromatography -- 2.1.5.3 SDS-PAGE -- 2.1.6 Purification of Proteins Based on Charge -- 2.1.6.1 Ion-Exchange Chromatography -- 2.1.6.2 Isoelectric Focusing -- 2.1.6.3 Polyacrylamide Gel Electrophoresis -- 2.1.7 Purification of Proteins Based on Polarity (Hydrophobic Interaction Chromatography) -- 2.1.8 Purification of Proteins Based on the Binding Property (Affinity Chromatography) |
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2.2 Biophysical and Biochemical Characterization of Protein -- 2.2.1 Biophysical Characterization Methods -- 2.2.2 Dynamic Light Scattering (DLS) -- 2.2.2.1 Applications of DLS -- 2.2.3 Circular Dichroism (CD) Spectroscopy -- 2.2.3.1 Applications of CD -- 2.2.3.2 Advantages of CD -- 2.2.4 Differential Scanning Calorimetry (DSC) -- 2.2.4.1 Applications of DSC -- 2.2.5 Fourier-Transform Infrared (FTIR) Spectroscopy -- 2.2.5.1 Advantages of FTIR -- 2.2.6 Isothermal Titration Calorimetry (ITC) -- 2.2.6.1 Applications of ITC -- 2.2.7 Biochemical Characterization -- 2.2.8 Oxidation -- 2.2.9 Deamidation |
| Summary |
This book discusses a broad range of basic and advanced topics in the field of protein structure, function, folding, flexibility, and dynamics. Starting with a basic introduction to protein purification, estimation, storage, and its effect on the protein structure, function, and dynamics, it also discusses various experimental and computational structure determination approaches; the importance of molecular interactions and water in protein stability, folding and dynamics; kinetic and thermodynamic parameters associated with protein-ligand binding; single molecule techniques and their applications in studying protein folding and aggregation; protein quality control; the role of amino acid sequence in protein aggregation; muscarinic acetylcholine receptors, antimuscarinic drugs, and their clinical significances. Further, the book explains the current understanding on the therapeutic importance of the enzyme dopamine beta hydroxylase; structural dynamics and motions in molecular motors; role of cathepsins in controlling degradation of extracellular matrix during disease states; and the important structure-function relationship of iron-binding proteins, ferritins. Overall, the book is an important guide and a comprehensive resource for understanding protein structure, function, dynamics, and interaction |
| Subject |
Proteins.
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Proteins -- Structure
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Proteins -- Conformation.
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Enzymes.
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Protein Conformation
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Protein Folding
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Proteins
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Enzymes
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protein.
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enzyme.
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Proteins -- Structure
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Bioinformatics
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Enzymology
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Medical genetics
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Proteins
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| Form |
Electronic book
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| Author |
Singh, Dev Bukhsh, editor
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Tripathi, Timir, editor
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| ISBN |
9789811555305 |
|
9811555303 |
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