Protein interface

Ebook "Protein-Protein interactions (Topics in Medicinal chemistry, Volume 8)" surveys the field of inhibitors of the MDM2/p53 interaction, which essentially began with the high-profile disclosure of Nutlins, and quickly and steadily grew through programs at a number of pharmaceutical companies. The MDM2/p53 interaction constitutes a paradigm example of a relatively large, hydrophobic interaction surface for which lead compounds can easily be found.

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Ebook "Disruption of protein–protein interfaces: In search of new inhibitors" reviews the latest developments and future perspectives in drug discovery at protein-protein interfaces. The authors detail experimental and computational tools to tackle the subject and highlight the contribution of the Italian research community to the field. Evidence shows that blocking or modulating protein-protein interactions might lead to the development of useful new drugs.

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Ebook "QCM-D studies on polymer behavior at interfaces" reviews the applications of quartz crystal microbalance with dissipation (QCM-D) in polymer research, including the conformational change of grafted polymer chains, the grafting kinetics of polymer chains, the growth mechanism of polyelectrolyte multilayers, and the interactions between polymers and phospholipid membranes.

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In ebook "Prion proteins (Topics in current chemistry, Volume 305)" we have assembled a set of chapters highlighting various aspects of prion diseases in humans and animals which show the intriguing features of both physiological and pathogenic PrP conformers. In addition, a wide spectrum of methodological approaches are described, ranging from in silico, chemical, and in vitro approaches to animal models, to illustrate the elaborate and extensive technology established in the prion field, allowing the analysis of disease mechanisms and the development of diagnostic and therapeutic strategies.

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Part 2 book "Dengue and dengue hemorrhagic fever" includes content: Taxonomy and evolutionary relationships of flaviviruses; molecular virology of dengue virus; the structural biology of dengue virus; the nonstructural proteins of dengue virus; the interface between dengue virus and the human host; dengue virus–mosquito interactions and molecular methods of vector control; animal models of dengue infection and disease;.... and other contents.

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This paper examines how molecular weight affects the diffusion of molecules in the interface of laminar flow in a microfluidic channel. Two mixtures of PS with anisole and PEG were used to evaluate the effect of molecular weight on the microfluidic separation.

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Embryonic mortality is a major concern in the commercial swine industry and primarily occurs early in gestation, but also during mid-gestation (~ days 50–70). Previous reports demonstrated that the embryonic loss rate was significant lower in Meishan than in commercial breeds (including Duroc). Most studies have focused on embryonic mortality in early gestation, but little is known about embryonic loss during mid-gestation.

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Many important cellular processes are carried out by protein complexes. To provide physical pictures of interacting proteins, many computational protein-protein prediction methods have been developed in the past.

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Protein interactions play a key role in life processes. Characterization of conformational properties of protein-protein interactions is important for understanding the mechanisms of protein association. The rapidly increasing amount of experimentally determined structures of proteins and protein-protein complexes provides foundation for research on protein interactions and complex formation.

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Molecular recognition in proteins occurs due to appropriate arrangements of physical, chemical, and geometric properties of an atomic surface. Similar surface regions should create similar binding interfaces. Effective methods for comparing surface regions can be used in identifying similar regions, and to predict interactions without regard to the underlying structural scaffold that creates the surface.

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Distinguishing biologically relevant interfaces from lattice contacts in protein crystals is a fundamental problem in structural biology. Despite efforts towards the computational prediction of interface character, many issues are still unresolved.

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Binding free energy and binding hot spots at protein-protein interfaces are two important research areas for understanding protein interactions. Computational methods have been developed previously for accurate prediction of binding free energy change upon mutation for interfacial residues.

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Transient protein-protein interactions (PPIs), which underly most biological processes, are a prime target for therapeutic development. Immense progress has been made towards computational prediction of PPIs using methods such as protein docking and sequence analysis.

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Protein–protein interactions can be seen as a hierarchical process occurring at three related levels: Proteins bind by means of specific domains, which in turn form interfaces through patches of residues.

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Since proteins function by interacting with other molecules, analysis of protein-protein interactions is essential for comprehending biological processes. Whereas understanding of atomic interactions within a complex is especially useful for drug design, limitations of experimental techniques have restricted their practical use. Despite progress in docking predictions, there is still room for improvement.

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The identification of protein-protein interaction sites is a computationally challenging task and important for understanding the biology of protein complexes. There is a rich literature in this field. A broad class of approaches assign to each candidate residue a real-valued score that measures how likely it is that the residue belongs to the interface.

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Various methods have been developed to computationally predict hotspot residues at novel proteinprotein interfaces. However, there are various challenges in obtaining accurate prediction. We have developed a novel method which uses different aspects of protein structure and sequence space at residue level to highlight interface residues crucial for the protein-protein complex formation.

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Bioactive cyclic peptides derived from natural sources are well studied, particularly those derived from non-ribosomal synthetases in fungi or bacteria. Ribosomally synthesised bioactive disulphide-bonded loops represent a large, naturally enriched library of potential bioactive compounds, worthy of systematic investigation.

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The physical interactions between proteins constitute the basis of protein quaternary structures. They dominate many biological processes in living cells. Deciphering the structural features of interacting proteins is essential to understand their cellular functions.

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Structural comparison of protein-protein interfaces provides valuable insights into the functional relationship between proteins, which may not solely arise from shared evolutionary origin. A few methods that exist for such comparative studies have focused on structural models determined at atomic resolution, and may miss out interesting patterns present in large macromolecular complexes that are typically solved by low-resolution techniques.

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