Frontiers in protein structure, function, and dynamics

著者

    • Singh, Dev Bukhsh
    • Tripathi, Timir

書誌事項

Frontiers in protein structure, function, and dynamics

Dev Bukhsh Singh, Timir Tripathi, editors

Springer, c2020

大学図書館所蔵 件 / 全3件

この図書・雑誌をさがす

注記

Includes bibliographical references

収録内容

  • 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
  • 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
  • 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 theBinding Property (Affinity Chromatography)
  • 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

内容説明・目次

内容説明

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.

目次

Chapter 1_ Protein purification, estimation, storage and their effect on structure, function and dynamics.- Chapter 2_Molecular motor: Subdomain dynamics and mechanochemistry.- Chapter 3_Computational insights into the role of SNPs/mutations in enzyme inhibition: progress and challenges.-Chapter 4_Use of group specific reagents in active site functional group elucidation.- Chapter 5_Understanding the potential role of structurally distant amino acids in modulating the structure and activity of proteins.- Chapter 6_Role of human genetic variations in the modulation of enzyme efficacy and activity of metabolic and xenobiotic metabolizing enzymes.- Chatper 7_Computational protein structure modeling: The gateway for drug design.- Chapter 8_Molecular dynamics simulation study of protein and protein-ligand complexes.- Chapter 9_Protein-protein interactions modeling: from wet to dry lab approaches

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