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Title Molecular biology of assemblies and machines / Alasdair C. Steven, Wolfgang Baumeister, Louise N. Johnson, Richard N. Perham.
Imprint New York : Garland Science, Taylor & Francis Group, [2016]


 Internet  Electronic Book    AVAILABLE
Description 1 online resource
Note Available only to authorized UTEP users.
Bio/Hist Note Wolfgang Baumeister is Director and Head of the Department of Structural Biology at the Max Planck-Institute of Biochemistry in Martinsried, Germany. Baumeister studied biology, chemistry and physics at the Universities of M nster and Bonn and obtained his PhD from the University of D'sseldorf. In 1973, he began his career as Research Associate in the Department of Biophysics at the University of D'sseldorf and held a Heisenberg Fellowship spending time at the Cavendish Laboratory in Cambridge, England. In 1982 he became a Group Leader at the Max-Planck-Institute of Biochemistry in Martinsried, Germany and then appointed Director and Head of the Department of Structural Biology. Baumeister pioneered the development of cryo-electron tomography and his work has shaped the understanding of the structure and function of the cellular machinery of protein degradation. His awards include the Otto Warburg Medal, the Schleiden Medal, the Louis-Jeantet Prize for Medicine, the Stein and Moore Award, the Harvey Prize in Science and Technology and the Ernst Schering Prize. He is a member of several academies including the US National Academy of Sciences and the American Academy of Arts and Sciences. Louise N. Johnson was an Emeritus Fellow of the Corpus Christi College at the University of Oxford in Cambridge, UK. Johnson was educated at University College, London, and began her postgraduate career at the Royal Institution working with Lawrence Bragg and David Phillips. There she co-discovered the structure of lysozyme in 1965, then the second protein and first enzyme ever solved by X-ray crystallography. As the David Phillips Professor of Molecular Biophysics at Oxford from 1990 to 2007, Johnson led structural studies of regulatory proteins of the cell cycle, protein kinases, and glycogen metabolism, crucial to understanding the origin of disease and new drug design. In 1976, together with Tom Blundell, she coauthored the widely infl
Subject Macromolecules.
Genre Electronic books.
Contents Cover; Half Title; Title Page; Copyright Page; Foreword; Preface; Acknowledgments; Contents; Special Features; Detailed Contents; Life Processes are Driven by Macromolecular Assemblies and Machines; Chapter 1 The Machines and Assemblies of Life; 1.1 EXPRESSION OF THE GENETIC BLUEPRINT; The flow of information is not perfect and not always in one direction; 1.2 WEAK FORCES AND MOLECULAR INTERACTIONS; All weak forces other than hydrophobic interactions are electrostatic in origin; Hydrophobic interactions drive the folding and assembly of macromolecules
The energy balance in folding and assembly has both enthalpic and entropic contributionsSize and topography matter for interaction patches; A certain minimum strength of interaction is required for specificity; Cooperativity enhances stability in multi-subunit complexes; 1.3 PROTEIN FOLDING AND STABILITY; Protein folding follows pathways populated with intermediates; Protein structures are only marginally stable; Protein stability correlates with size and other factors such as covalent cross-links; Many cellular proteins denature collectively under thermal stress
Proteins from thermophilic organisms are not very different from mesophilic homologs1.4 SELF-ASSEMBLY AND SYMMETRY; Most proteins form symmetrical oligomers with two or more subunits; Symmetry defines a set of larger structures composed of multiple copies of identical subunits; Line and cyclic point group symmetries generate helices and rings; Cubic symmetry is employed in a variety of oligomeric proteins; Assembly proceeds along pathways; Why are there so many large macromolecular assemblies?; 1.5 MACROMOLECULAR DYNAMICS; Ensemble methods measure the net signal from numerous contributors
'Single-molecule' methods interrogate macromolecules one at a timeMolecular dynamics models the motions of crystal structures in the presence of a force field; 1.6 CATALYSIS; Enzymes form highly specific but transient complexes with their substrates; Enzyme kinetics are governed by a few equations; A key feature of enzyme catalysis is the tight binding of the transition state; Enzymes generate catalytic rate enhancements in multiple ways; Enzymes can be inhibited reversibly and irreversibly; Coupling of enzyme-catalyzed reactions allows energetically unfavorable reactions to occur
1.7 SIGNALING AND REGULATORY MECHANISMSLigand-induced conformational change and cooperativity are widespread methods of controlling biological activity; Allosteric proteins are regulated by a special form of cooperativity; Allosteric enzymes do not follow Michaelis-Menten kinetics; Allostery is mediated by protein/protein interactions and conformational changes; Reversible covalent modification controls the activities of some proteins; Homeostasis is an important aspect of response to environmental change; 1.8 MACROMOLECULAR CROWDING
Summary Molecular Biology of Assemblies and Machines presents a comprehensive narrative describing the structures of macromolecular complexes and how they assemble and interact. Richly illustrated, it is written for advanced undergraduates, graduate students, and researchers in biochemistry, structural biology, molecular biology, biophysics, cell biology,
Other Author Baumeister, W. (Wolfgang), 1946- author.
Johnson, L. N., author.
Perham, R. N., author.
Other Title Print version: 9780815341666 0815341660