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Fuzziness
  • Language: en
  • Pages: 210

Fuzziness

Detailed characterization of fuzzy interactions will be of central importance for understanding the diverse biological functions of intrinsically disordered proteins in complex eukaryotic signaling networks. In this volume, Peter Tompa and Monika Fuxreiter have assembled a series of papers that address the issue of fuzziness in molecular interactions. These papers provide a broad overview of the phenomenon of fuzziness and provide compelling examples of the central role played by fuzzy interactions in regulation of cellular signaling processes and in viral infectivity. These contributions summarize the current state of knowledge in this new field and will undoubtedly stimulate future research that will further advance our understanding of fuzziness and its role in biomolecular interactions.

Theory and Applications of the Empirical Valence Bond Approach
  • Language: en
  • Pages: 284

Theory and Applications of the Empirical Valence Bond Approach

A comprehensive overview of current empirical valence bond (EVB) theory and applications, one of the most powerful tools for studying chemical processes in the condensed phase and in enzymes. Discusses the application of EVB models to a broad range of molecular systems of chemical and biological interest, including reaction dynamics, design of artificial catalysts, and the study of complex biological problems Edited by a rising star in the field of computational enzymology Foreword by Nobel laureate Arieh Warshel, who first developed the EVB approach

Intrinsically Disordered Proteins
  • Language: en
  • Pages: 73

Intrinsically Disordered Proteins

  • Type: Book
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  • Published: 2014-08-05
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  • Publisher: Springer

In this brief, Vladimir Uversky discusses the paradigm-shifting phenomenon of intrinsically disordered proteins (IDPs) and hybrid proteins containing ordered domains and functional IDP regions (IDPRs). Beginning with an introduction to the concept of protein intrinsic disorder, Uversky then goes on to describe the peculiar amino acid sequences of IDPs, their structural heterogeneity, typical functions and disorder-based binding modes. In the final sections, Uversky discusses IDPs in human diseases and as potential drug targets. This volume provides a snapshot to researchers entering the field as well as providing a current overview for more experienced scientists in related areas.

The Spiritual Life of Water
  • Language: en
  • Pages: 330

The Spiritual Life of Water

Water’s wisdom on renewal, communication, and holism • How water, as a conscious organism, unites all of creation in one vast communication network • Includes the research of Masaru Emoto and Viktor Schauberger • Discusses the energetics of water, water treatments, finding the best-quality water, and the perils of bottled and distilled water Once held sacred the world over, water contains a wisdom few today acknowledge. Driving everything from our metabolic processes to weather patterns and climate change, its real significance lies in its role as a medium for metamorphosis, recycling, and exchanging energy and information. Seeking a return to our ancestors’ reverence for water, Al...

Structural Bioinformatics of Membrane Proteins
  • Language: en
  • Pages: 287

Structural Bioinformatics of Membrane Proteins

This book is the first one specifically dedicated to the structural bioinformatics of membrane proteins. With a focus on membrane proteins from the perspective of bioinformatics, the present work covers a broad spectrum of topics in evolution, structure, function, and bioinformatics of membrane proteins focusing on the most recent experimental results. Leaders in the field who have recently reported breakthrough advances cover algorithms, databases and their applications to the subject. The increasing number of recently solved membrane protein structures makes the expert coverage presented here very timely. Structural bioinformatics of membrane proteins has been an active area of research over the last thee decades and proves to be a growing field of interest.

Unfolded Proteins
  • Language: en
  • Pages: 330

Unfolded Proteins

The word revolution has a number of definitions (The American Heritage Dictionary, 2006). The one most pertinent to this series and volume is 'a sudden or momentous change in a situation'. Recent years have seen an unprecedented explosion of interest in unfolded proteins in all of their various forms. Coupled with this increase in interest we have seen momentous changes in the way unfolded proteins are viewed. Two particular paradigms have come under close scrutiny: unfolded proteins are disordered random coils devoid of persistent structure, and protein function first requires protein structure. The first of these is currently a hotly debated subject. The second paradigm we can safely claim...

On protein structure, function and modularity from an evolutionary perspective
  • Language: en
  • Pages: 206

On protein structure, function and modularity from an evolutionary perspective

We are compounded entities, given life by a complex molecular machinery. When studying these molecules we have to make sense of a diverse set of dynamical nanostructures with wast and intricate patterns of interactions. Protein polymers is one of the major groups of building blocks of such nanostructures which fold up into more or less distinct three dimensional structures. Due to their shape, dynamics and chemical properties proteins are able to perform a plethora of specific functions essential to all known cellular lifeforms. The connection between protein sequence, translated into protein structure and in the continuation into protein function is well accepted but poorly understood. Malf...

Computational Protein-Protein Interactions
  • Language: en
  • Pages: 346

Computational Protein-Protein Interactions

  • Type: Book
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  • Published: 2009-06-26
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  • Publisher: CRC Press

Often considered the workhorse of the cellular machinery, proteins are responsible for functions ranging from molecular motors to signaling. The broad recognition of their involvement in all cellular processes has led to focused efforts to predict their functions from sequences, and if available, from their structures. An overview of current resear

Weak Interactions in Molecular Machinery
  • Language: en
  • Pages: 105

Weak Interactions in Molecular Machinery

Diverse cellular processes depend on weak interactions between biological components. In this volume, we bring together a wealth of recent information on this topic, combining original research articles with up-to-date reviews, organized under four separate themes. In our first section on nucleic acid regulation, we include a study of the PII-NAGK-PipX-NtcA regulatory axis of cyanobacteria and discover much about the role of RNA binding protein regulation and cross-talk in the control of AU-rich mRNA. Peptide-mediated weak interactions are our second theme in which we review weak molecular interactions in clathrin-mediated endocytosis, investigate the selectivity of the G7-18NATE inhibitor p...

Caveolins and Caveolae
  • Language: en
  • Pages: 199

Caveolins and Caveolae

Caveolae are 50-100 nm flask-shaped invaginations of the plasma membrane that are primarily composed of cholesterol and sphingolipids. Using modern electron microscopy techniques, caveolae can be observed as omega-shaped invaginations of the plasma membrane, fully-invaginated caveolae, grape-like clusters of interconnected caveolae (caveosome), or as transcellular channels as a consequence of the fusion of individual caveolae. The caveolin gene family consists of three distinct members, namely Cav-1, Cav-2 and Cav-3. Cav-1 and Cav-2 proteins are usually co-expressed and particularly abundant in epithelial, endothelial, and smooth muscle cells as well as adipocytes and fibroblasts. On the other hand, the Cav-3 protein appears to be muscle-specific and is therefore only expressed in smooth, skeletal and cardiac muscles. Caveolin proteins form high molecular weight homo- and/or hetero-oligomers and assume an unusual topology with both their N- and C-terminal domains facing the cytoplasm.