TY  - BOOK
AU  - Erickson,Harold P.
ED  - Institute of Physics (Great Britain),
TI  - Principles of protein-protein association
T2  - [IOP release 6]
SN  - 9780750324120
AV  - QP551.5 .E757 2019eb
U1  - 572/.64 23
PY  - 2019///]
CY  - Bristol [England] (Temple Circus, Temple Way, Bristol BS1 6HG, UK)
PB  - IOP Publishing
KW  - Protein-protein interactions
KW  - Proteins
KW  - physiology
KW  - Protein Interaction Mapping
KW  - Biophysics
KW  - bicssc
KW  - SCIENCE / Life Sciences / Biophysics
KW  - bisacsh
N1  - "Version: 20190601"--Title page verso; Includes bibliographical references; 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 s; 2. Basic thermodynamics of reversible association -- 3. The nature of the protein-protein bond, �a 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; 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 interf; 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, an; 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. Ha; 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; 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 pr; Graduate students in biochemistry and cell biology; Also available in print
N2  - 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
UR  - https://ezproxy.mef.edu.tr/login?url=https://iopscience.iop.org/book/978-0-7503-2412-0
ER  -