By Martin Zacharias
ISBN-10: 184816338X
ISBN-13: 9781848163386
ISBN-10: 1848163398
ISBN-13: 9781848163393
Given the great growth completed in elucidating protein–protein complicated buildings and within the box of protein interplay modeling, there's nice call for for a e-book that provides researchers/students a finished evaluation of the sphere. This e-book does simply that. It specializes in what should be discovered approximately protein–protein interactions from the research of protein–protein complicated constructions and interfaces. What are the riding forces for protein–protein organization? How do we extract the mechanism of particular reputation from learning protein–protein interfaces? How can this data be used to foretell and layout protein–protein interactions (interaction areas and intricate structures)? What tools are at present hired to layout protein–protein interactions, and the way do we impact protein–protein interactions by way of mutagenesis and small-molecule medicinal drugs or peptide mimetics? The booklet includes approximately 15 assessment chapters, written by way of specialists, at the characterization of protein–protein interfaces, constitution choice of protein complexes (by Nmr and X-ray), idea of protein–protein binding, dynamics of protein interfaces, bioinformatics the right way to are expecting interplay areas, and prediction of protein–protein complicated buildings (docking and homology modeling of complexes, etc.) and layout of protein–protein interactions. It serves as a bridge among studying/analyzing protein–protein advanced constructions (interfaces), predicting interactions, and influencing/designing interactions.
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Extra resources for Protein, Protein Complexes: Analysis, Modeling and Drug Design
Example text
Atomic packing and surface complementarity. 1 for 122 homodimeric proteins, 70 protein–protein complexes, and 188 crystal packing interfaces with a BSA > 800 Å2. All have been scaled to 1 for the homodimer interfaces. Comparatively low values of the Sc shape complementarity index, of the reciprocal of the Igap gap volume index, of the LD packing index, and of the fbu fraction of buried atoms, all confirm that the atomic packing is less compact and the surface complementarity less good in crystal packing interfaces.
E. (1998). Biophys J 74: 546–558. 55. E. (2007). J Mol Biol 369: 541–552. 56. , Chakrabarti P. (2008). Quart Rev Biophysics 41: 1–48. CHAPTER 3 Energetics of Protein–Protein Interactions Ilian Jelesarov Department of Biochemistry, University of Zurich, Winterthurerstr. ch Proteins have evolved as versatile components of the molecular organisation of life. Formation of protein–protein complexes is indispensable in maintaining the organisation and integration of practically all biological processes.
54 explained the assembly pathways of three icosahedral viruses with the help of van der Waals and electrostatic association energies calculated for each pairwise unique interface. 55 detected assembly intermediates and investigated the formation of a whole T = 3 bacteriophage MS2 capsid by using the electrospray ionization–mass spectrometry. 17 explain the assembly process of HK97. 23 They also identified ‘medium’ size interfaces formed between pentamers and hexamers, and also between pairs of hexamers which are related either by icosahedral or quasi 2- or 3-fold symmetry.
Protein, Protein Complexes: Analysis, Modeling and Drug Design by Martin Zacharias
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