Principles of protein-protein association /

Protein-protein associations are fundamental to biological mechanisms, creating a need for a book that covers the basic principles of protein-protein association. This book has been developed from lectures given to graduate students in cell and molecular biology. The general principles are accompani...

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Detalles Bibliográficos
Clasificación:Libro Electrónico
Autor principal: Erickson, Harold P. (Autor)
Formato: Electrónico eBook
Idioma:Inglés
Publicado: Bristol [England] (Temple Circus, Temple Way, Bristol BS1 6HG, UK) : IOP Publishing, [2019]
Colección:IOP (Series). Release 6.
IOP expanding physics.
Biophysical Society series.
Temas:
Protein-protein interactions.
Proteins > physiology.
Protein Interaction Mapping.
Biophysics.
SCIENCE / Life Sciences / Biophysics.
Acceso en línea:Texto completo
Tabla de Contenidos:
  • 1. Size and shape of protein molecules at the nm level determined by sedimentation, gel filtration and electron microscopy
  • 1.1. Introduction
  • 1.2. How big is a protein molecule?
  • 1.3. How far apart are molecules in solution?
  • 1.4. The sedimentation coefficient and frictional ratio. Is the protein globular or elongated?
  • 1.5. The Kirkwood/Bloomfield calculation
  • 1.6. Gel filtration chromatography and the Stokes radius
  • 1.7. Determining the molecular weight of a protein molecule--combining S and Rs à la Siegel and Monte
  • 1.8. Electron microscopy of protein molecules
  • 1.9. Hydrodynamic analysis and EM applied to large multi-subunit complexes
  • 2. Basic thermodynamics of reversible association
  • 3. The nature of the protein-protein bond, à la Chothia and Janin
  • 3.1. Hydrogen bonds and ionic bonds in proteins
  • 3.2. The simplified protein bond model of Chothia and Janin
  • 3.3. The hydrophobic bond
  • 3.4. Complementarity
  • 3.5. Final comments : what is the mechanical rigidity of globular proteins and their polymers?
  • 4. The structure of an antibody bound to its protein ligand--lock and key versus induced fit and conformational selection
  • 4.1. Nature's site-directed mutagenesis experiment
  • 4.2. Induced fit and conformational selection
  • 5. The complex of growth hormone with its receptor--one protein interface binds two partners
  • 5.1. GHR binds two different patches on opposite sides of GH
  • 5.2. Other proteins with multiple binding partners
  • 6. The hot spot in protein-protein interfaces
  • 6.1. Hot spot paper one--the technology and alanine scanning of GH
  • 6.2. Hot spot paper two--scanning GHR and matching the hot spots
  • 6.3. Plasticity in the evolution of protein-protein interfaces
  • 6.4. Trying to predict hot spot amino acids, and protein-protein interfaces
  • 7. Cooperativity in protein-protein association and efficiency of bonds
  • 7.1. Intrinsic bond energy and subunit entropy
  • 7.2. Additivity of bond energies and cooperative association
  • 7.3. Analysis of cooperativity in GH-GHR association, and comments on the 'efficiency' of hydrophobic bonding
  • 7.4. Conclusions
  • 8. Kinetics of protein-protein association and dissociation
  • 8.1. What is the half time of the empty receptor?
  • 8.2. What is the half time of the complex?
  • 8.3. The diffusion-limited rate constant for protein-protein association
  • 8.4. Half time of the empty receptor and the complex--guessing the kinetics
  • 8.5. Proteins can associate much slower and much faster than the diffusion-limited rate
  • 9. Techniques for measuring protein-protein association--use and misuse of ELISA
  • 9.1. Qualitative assays to screen for protein-protein association in vivo
  • 9.2. Quantitative methods for measuring the KD of protein-protein association
  • 9.3. Assays that can be done in most laboratories
  • 9.4. Assays requiring specialized equipment and expertise
  • 9.5. Fitting the binding data to determine KD
  • 9.6. ELISA--use and misuse
  • 9.7. A simple ELISA can over- or under-estimate the KD by orders of magnitude
  • 9.8. A competitive ELISA can be used to measure the true KD
  • 10. Fibronectin, the FNIII domain, and artificial antibodies
  • 10.1. Fibronectin, cell adhesion and RGD
  • 10.2. Antibody mimics--creating novel binding activities in a neutral protein framework
  • 11. Association of intrinsically disordered proteins--flexible binding partners.

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