1 edition of Protein dimerization and oligomerization in biology found in the catalog.
Protein dimerization and oligomerization in biology
Jacqueline M. Matthews
Includes bibliographical references and index.
|Statement||edited by Jacqueline M. Matthews|
|Series||Advances in experimental medicine and biology -- v. 747, Advances in experimental medicine and biology -- v. 747.|
|The Physical Object|
|LC Control Number||2012005555|
Interestingly, the peptide was shown to switch its oligomerization state from a dimer to a trimer upon increasing ionic strength. The correctness of the rational design principles used here is supported by details of the atomic structure of the peptide deduced from X-ray crystallography. Through the biochemical characterization of LRRK2 protein, we find that kinase activity is dependent on dimerization whereas further oligomerization results in a loss of activity. We develop a Bimolecular Fluorescence (BiFC) assay based on eGFP fluorescence dependent on protein dimerization.
Abstract Protein‐protein interactions, including oligomerization, are involved in regulation of many cellular processes. Unfortunately, many proteins are expressed at a very low level in vivo, making it challenging to observe oligomerization by size‐exclusion chromatography, also known as gel filtration. Protein dimerization or oligomerization is a key factor in signal transduction process. It is of great significance to develop novel strategies for investigating protein dimerization in cells and in vivo. Herein, we report a nongenetic proximity-induced fluores-cence resonance energy transfer (FRET) strategy based on DNA tetrahedron for visualizing the receptor dimerization. In this nano.
Therefore, regulating receptor oligomerization provides an opportunity to customize cellular signaling and to direct cellular behavior in a user-defined manner. Some techniques have been developed for receptor oligomerization regulation, such as chemically induced dimerization (CID) and optogenetics, which involve traditional genetic engineering. INTRODUCTION. Oligomerization is one of the fundamental principles by which nature creates versatile biologically relevant systems (1–3).At the submolecular level, two, three, or four α-helical strands can pack parallel or antiparallel to form a bundle called a coiled-coil, which is widespread in protein structures (1, 4).At the intermolecular level, multiple proteins can cluster into homo.
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The Detection and Quantitation of Protein Oligomerization. David A. Gell, Richard P. Grant, Joel P. Mackay. Pages Computational and Structural Characterisation of Protein Associations. Susan Jones. Pages Death by Caspase Dimerization. Sarah H. MacKenzie, A. Clay Clark. Pages Protein Dimerization and Oligomerization in Biology (Advances in Experimental Medicine and Biology ()): Medicine & Health Science Books @ mat: Hardcover.
Covers many aspects of hetero-oligomerization. Gives comprehensive overview of the contributions of protein dimer and oligomer formation to nucleic acid binding. Provides an overview of repeat proteins. see more benefits. Buy this book. eBook ,79 €. price for Spain (gross) Buy eBook.
ISBN. Protein dimerization and oligomerization in biology. [Jacqueline M Matthews;] -- "This volume has a strong focus on homo-oligomerization, which is surprisingly common.
However, protein function is so often linked to both homo- and hetero-oligomerization and many heterologous. Get this from a library. Protein dimerization and oligomerization in biology.
[Jacqueline M Matthews;] -- "This volume has a strong focus on homo-oligomerization, which is surprisingly common. However, protein function is so often linked to both homo- and hetero-oligomerization and many heterologous. Protein dimerization and higher-order oligomerization are prevalent mechanisms used to modulate diverse biological functions, including enzyme activity, transcription regulation, DNA processing.
The protein chains are shown in ribbons of different colors. For a few amino acids, all atoms are indicated in balls and sticks to highlight intra and inter atomic interactions. Recognition modes. A protein interface is made of two set of atoms, one per chain, spatially organized to yield a chemical and geometrical complementarity.
The power of two: protein dimerization in biology. The self-association of proteins to form dimers and higher-order oligomers is a very common phenomenon. Recent structural and biophysical studies show that protein dimerization or oligomerization is a key factor in the regulation of proteins such as enzymes, ion channels, receptors and transcription by: Description: This book is interdisciplinary, it covers fields from organic chemistry to mathematics, and raises different aspects of oligomerization.
It is a great source of information as every chapter introduces general knowledge and deep details. Sergio Barranco-Medina, Karl-Josef Dietz, in Methods in Enzymology, Oligomerization is a frequently encountered physical characteristic of biological molecules that occurs for a wide number of transcription factors, ion channels, oxygen-carrying macromolecules such as hemocyanin and enzymes.
On the other hand, unwanted protein oligomerization can lead to the formation of pathogenic. Oligomerization and Allosteric Modulation in G-Protein Coupled Receptors (Volume ) (Progress in Molecular Biology and Translational Science (Volume )): Medicine & Health Science Books @ Moreover, recent studies on the identified AßP species have indicated that the oligomerization of AßP and the conformational changes are critical in the neurodegeneration process.
AßP is a small peptide of 39–43 amino acid long. It is derived from the proteolytic cleavage of a large precursor protein (amyloid precursor protein; APP). MacKenzie S.H., Clark A.C.
() Death by Caspase Dimerization. In: Matthews J.M. (eds) Protein Dimerization and Oligomerization in Biology. Advances in Experimental Medicine and Biology, vol Recent structural and biophysical studies show that protein dimerization or oligomerization is a key factor in the regulation of proteins such as enzymes, ion channels, receptors and transcription factors.
In addition, self-association can help to minimize genome size, while maintaining the advantages of modular complex formation.
The self-association of proteins to form dimers and higher-order oligomers is a very common phenomenon. Recent structural and biophysical studies show that protein dimerization or oligomerization is a key factor in the regulation of proteins such as enzymes, ion.
We studied parallel G4-mediated protein dimerization and activation by incorporating a RHAU peptide with a fluorescent protein FRET pair CFP/YFP and an apoptotic casp9.
Occurrence of energy tranfer (from donor CFP to acceptor YFP) and enhancement of fold cleavage efficiency of casp9 were observed in the presence. G protein coupled receptors (GPCRs) play essential roles in intercellular communication.
Although reported two decades ago, the assembly of GPCRs into dimer and larger oligomers in. G protein‐coupled receptors are one of the most actively studied families of proteins.
However, despite the ubiquity of protein dimerization and oligomerization as a structural and functional motif in biology, until the last decade they were generally considered as monomeric, non‐interacting polypeptides. Understanding how these oligomeric complexes are assembled is thus a central topic in biophysics and molecular biology.
Several studies have investigated the kinetics and thermodynamics of protein oligomerization, and different kinetic mechanisms have been identified (3, 4). However, current understanding of the assembly mechanism is still limited.
Gell, DA and Grant, RP and Mackay, JP, The detection and quantitation of protein oligomerization, Advances in Experimental Medicine and Biology: Protein Dimerization and Oligomerization in Biology, Springer, JM Matthews (ed), New York, United States, pp.
ISBN () [Research Book Chapter] Item Details. Identifying Mechanisms of Dimerization. We obtained 4, pairs of a dimer and a closest monomer from the same Conserved Domain Database (CDD) family for the full dataset and pairs for the nonredundant dataset (see Materials and Methods).This list contained different CDD families ( families in the nonredundant dataset) encompassing a wide range of protein biological ./ Oligonucleotide binding proteins: the occurrence of dimer and multimer formation.
Protein Dimerization and Oligomerization in Biology. editor / J M Matthews. 1st. ed. USA:. The RelA protein of Escherichia coli is a ribosome-associated (p)ppGpp synthetase that is activated by amino acid deprivation.
It was recently reported that the activity of .