Large sized planar structures are increasingly being employed in satellite and radar applications. But due to large electrical size and complex cellular patterns of modern designs, full-wave analysis of these structures requires enormous memory and processing requirements. Therefore conventional techniques based on linear meshing either fail to simulate such structures or require resources not available to a common antenna designer. A novel technique called Scale-changing Technique (SCT) addresses this problem by partitioning the cellular array geometry in numerous nested domains defined at different scale-levels in the array plane. Multi-modal networks, called Scale-changing Networks (SCN), are then computed to model the electromagnetic interaction between any two successive partitions. The cascade of these networks allows the computation of the equivalent surface impedance matrix of the complete array which in turn can be utilized to compute far-field scattering patterns. Since the computation of scale-changing networks is mutually independent, execution times can be reduced significantly by employing multiple processing units.
Cellular anchors are large accumulations of a multitude of multi-functional proteins and are known as focal adhesion sites. In this work, the spatial organization of the cell-matrix proteins Beta3-integrin, Talin, Kindlin 1&2, FAK, Paxillin, Vinculin, Zyxin, Alpha-actinin and Actin was analyzed, using the super-resolution microscopy technique PALM. It was demonstrated, that all cell-matrix proteins form distinct areas of varying densities inside single focal adhesions. In order to study the temporal alterations and formation of highly dense protein accumulations, the dynamic behavior of the adhesion receptor Beta3-integrin was analyzed. It was shown, that force inhibition can induce structural rearrangements, also leading to the redistribution of the density inside adhesion sites. Dense domains could even have a particular signaling function, as it was demonstrated that the signaling protein FAK is primarily recruited to delimited areas inside focal adhesions, which could represent dense domains.
Artificial and natural instances of networks areubiquitous, and the problem of determining theoptimal topology of a network is of practical valueto many domains. Evolutionary algorithms constitute awell-established optimisation method, but they scalepoorly if applied to the combinatorial explosion ofpossible network topologies. Generativerepresentation schemes aim to overcome this problemby facilitating the discovery and reuse of designdependencies and allowing for adaptable explorationstrategies. This book seeks to define a simple yetuniversally applicable and scalable method forevolving graphs and networks. A number ofcontributions are made in this regard. We establishthe notion of directly evolving a graph grammar fromwhich a population of networks can be derived.Compact cellular productions that form a hypergraphgrammar are optimised by a novel multi-objectiveevolutionary design system. A series of empiricalinvestigations are then carried out to gain a betterunderstanding of graph grammar evolution.
Endocytosis is an essential cellular process requiredfor functions including nutrient uptake, membranerecycling, and signal transduction. In comparison tothe clathrin-mediated pathway, clathrin-independentpathways are poorly understood. New work is nowbeginning to reveal a picture of multiplenon-clathrin pathways. Findings presented in thisbook identify that ErbB2 is internalized through anon-clathrin pathway in geldanamycin-treated SKBr3human breast cancer cells. ErbB2 internalizationresembled a newly described non-clathrin pathwaytermed the GEEC pathway, a pathway thought to bespecific for internalization of GPI-anchoredproteins. Suprisingly, ErbB2 and GPI-anchoredproteins also co-localized with chimeric fusionproteins containing transmembrane domains, proteinsexpected to be excluded from the GEEC pathway. Combined with other data from the lab, these resultssuggest that this pathway is not specific forGPI-anchored proteins and may instead represent abulk internalization pathway.
Post-translational phosphorylation is one of the most common protein modifications that occur in animal cells. The vast majority of phosphorylation occurs as a mechanism of acute and reversible regulation of protein function. Studies of mammalian cells metabolically labeled with p32 orthophosphate suggest that as many as one-third of all cellular proteins are covalently modified by protein phosphorylation. Covalent attachment of a phosphate group to an amino acid side chain of a protein can cause a structural change, for example, by attracting a cluster of positively charged side chains. Such a change occurring at one site in a protein can in turn alter the protein s conformation elsewhere. Reversible protein phosphorylation is the predominant strategy used to control the activity of proteins in eukaryotic cells. The phosphates are transferred from ATP molecules by protein kinases and are taken off by protein phosphatases. In animal cells, serine, threonine and tyrosine are the amino acids subjected to phosphorylation. The protein kinases belong to a large family of enzymes, which contain a similar amino acid catalytic (kinase) domains.
The present study was focussed on the development of integrated database of bioactive peptides of milk proteins and other resources, in-silico study of the structures, phylogeny and conserved domains of different bioactive peptides. The developed the integrated database of different bioactive peptides viz. antithrombotic, antimicrobial, opioid, immunomodulatory, mineral binding peptides was developed. In present work, the back end of the above stated database was developed into MSAccess then front end is in JSP, JSS and HTML. This database will be helpful to the researchers working on bioactive peptides. It comprises an information associated to bioactive molecules like Gene-ID, common and scientific name etc. and has significant description of biological process, molecular function and cellular component. Subsequently, feasible structures of bioactive peptides were also designed by using homology approach. For this purpose online server of swiss modal, swiss templates along with swiss repository was used
Protein-protein interactions are extremely valuable towards protein functions and cellular processes or we can say that protein-protein interactions play an important role in living cells. Therefore, if we can control the interactions between proteins, as a result, we can control some functionality of cells. Main functionality of a protein is carried out by its domains. So, domain is a structural or/and functional unit of protein. Behind protein-protein interactions there exist some domain-domain interactions. Therefore, under standing protein-protein interaction at domain level gives a global view of protein-protein interaction network.In this book, we have made an attempt to infer domain-domain interactions from interacting and non-interacting protein pairs then we have predicted protein-protein interactions based on inferred domain-domain interactions.
Proper inheritance of DNA methylation patterns during cell division is critical for preserving cellular identity and preventing malignant cellular transformation. In humans, DNA methylation patterns are established during development and then maintained through multiple somatic cell divisions by co-operative activity of the de novo and maintenance DNA methyltransferases - DNMT3A/3B and DNMT1, respectively. A key question that remained unresolved is how the de novo DNMT3A/3B enzymes assist in faithful inheritance of methylation patterns in somatic cells while guarding against aberrant de novo DNA methylation. This study revealed a novel self-regulatory inheritance mechanism where DNMT3A/3B remain bound to nucleosomes containing methylated DNA, which stabilizes these proteins and enables faithful propagation of DNA methylation within the methylated domains through cooperative activity of DNMT3A/3B and DNMT1 enzymes. Such a mechanism not only ensures faithful somatic propagation of methylated states but also prevents aberrant de novo methylation by causing degradation of free DNMT3A/3B enzymes.
Closed Loop Neuroscience addresses the technical aspects of closed loop neurophysiology, presenting the implementation of these approaches spanning several domains of neuroscience, from cellular and network neurophysiology, through sensory and motor systems, and then clinical therapeutic devices.Although closed-loop approaches have long been a part of the neuroscientific toolbox, these techniques are only now gaining popularity in research and clinical applications. As there is not yet a comprehensive methods book addressing the topic as a whole, this volume fills that gap, presenting state-of-the-art approaches and the technical advancements that enable their application to different scientific problems in neuroscience.Presents the first volume to offer researchers a comprehensive overview of the technical realities of employing closed loop techniques in their workOffers application to in-vitro, in-vivo, and hybrid systemsContains an emphasis on the actual techniques used rather than on specific results obtainedIncludes exhaustive protocols and descriptions of software and hardware, making it easy for readers to implement the proposed methodologiesEncompasses the clinical/neuroprosthetic aspect and how these systems can also be used to contribute to our understanding of basic neurophysiologyEdited work with chapters authored by leaders in the field from around the globe - the broadest, most expert coverage available