Cargando…
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...
| Clasificación: | Libro Electrónico |
|---|---|
| Autor principal: | |
| 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: | |
| Acceso en línea: | Texto completo |
MARC
| LEADER | 00000nam a2200000 4500 | ||
|---|---|---|---|
| 001 | IOP_9780750324120 | ||
| 003 | IOP | ||
| 005 | 20190702210331.0 | ||
| 006 | m eo d | ||
| 007 | cr cn |||m|||a | ||
| 008 | 190702s2019 enka ob 000 0 eng d | ||
| 020 | |a 9780750324120 |q ebook | ||
| 020 | |a 9780750324113 |q mobi | ||
| 020 | |z 9780750324106 |q print | ||
| 024 | 7 | |a 10.1088/2053-2563/ab19ba |2 doi | |
| 035 | |a (CaBNVSL)thg00979231 | ||
| 035 | |a (OCoLC)1107216922 | ||
| 040 | |a CaBNVSL |b eng |e rda |c CaBNVSL |d CaBNVSL | ||
| 050 | 4 | |a QP551.5 |b .E757 2019eb | |
| 060 | 4 | |a QU 55 |b ER68p 2019eb | |
| 072 | 7 | |a PHVN |2 bicssc | |
| 072 | 7 | |a SCI009000 |2 bisacsh | |
| 082 | 0 | 4 | |a 572/.64 |2 23 |
| 100 | 1 | |a Erickson, Harold P., |e author. | |
| 245 | 1 | 0 | |a Principles of protein-protein association / |c Harold P. Erickson. |
| 264 | 1 | |a Bristol [England] (Temple Circus, Temple Way, Bristol BS1 6HG, UK) : |b IOP Publishing, |c [2019] | |
| 300 | |a 1 online resource (various pagings) : |b illustrations (some color). | ||
| 336 | |a text |2 rdacontent | ||
| 337 | |a electronic |2 isbdmedia | ||
| 338 | |a online resource |2 rdacarrier | ||
| 490 | 1 | |a [IOP release 6] | |
| 490 | 1 | |a IOP expanding physics, |x 2053-2563 | |
| 490 | 1 | |a Biophysical Society series | |
| 500 | |a "Version: 20190601"--Title page verso. | ||
| 504 | |a Includes bibliographical references. | ||
| 505 | 0 | |a 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 | |
| 505 | 8 | |a 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? | |
| 505 | 8 | |a 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 | |
| 505 | 8 | |a 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 | |
| 505 | 8 | |a 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 | |
| 505 | 8 | |a 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 | |
| 505 | 8 | |a 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 | |
| 505 | 8 | |a 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 | |
| 505 | 8 | |a 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. | |
| 520 | 3 | |a 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 accompanied by guided reading of informative classic papers. This book should be useful for faculties organizing similar classes, and also for students and researchers who wish to learn on their own. Part of the / Biophysical Society series. | |
| 521 | |a Graduate students in biochemistry and cell biology. | ||
| 530 | |a Also available in print. | ||
| 538 | |a Mode of access: World Wide Web. | ||
| 538 | |a System requirements: Adobe Acrobat Reader, EPUB reader, or Kindle reader. | ||
| 545 | |a Dr. Erickson is a Professor in the Departments of Cell Biology, Biochemistry and Biomedical Engineering at Duke University. Having received his PhD in biophysics from Johns Hopkins University in 1968, he did postdoctoral work with Aaron Klug at the MRC lab, Cambridge England, developing techniques for computer reconstruction of electron microscope images. His research career at Duke University has focused the cytoskeleton and extracellular matrix, with an emphasis on protein-protein associations and self-assembly. He has published more than 200 peer reviewed articles. | ||
| 588 | 0 | |a Title from PDF title page (viewed on July 2, 2019). | |
| 650 | 0 | |a Protein-protein interactions. | |
| 650 | 1 | 2 | |a Proteins |x physiology. |
| 650 | 1 | 2 | |a Protein Interaction Mapping. |
| 650 | 7 | |a Biophysics. |2 bicssc | |
| 650 | 7 | |a SCIENCE / Life Sciences / Biophysics. |2 bisacsh | |
| 710 | 2 | |a Institute of Physics (Great Britain), |e publisher. | |
| 776 | 0 | 8 | |i Print version: |z 9780750324106 |
| 830 | 0 | |a IOP (Series). |p Release 6. | |
| 830 | 0 | |a IOP expanding physics. | |
| 830 | 0 | |a Biophysical Society series. | |
| 856 | 4 | 0 | |u https://iopscience.uam.elogim.com/book/978-0-7503-2412-0 |z Texto completo |