Intrinsic protein disorder
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Intrinsic structural disorder is a common property of many proteins, especially in eukaryotic and virus proteomes. The tendency of some proteins or protein regions to exist in a disordered state usually precludes their structural characterisation and renders them especially difficult for experimental handling after recombinant expression.
9p viseulgi2711 31-08-2021 9 1 Download
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A number of proteins contain regions which do not adopt a stable tertiary structure in their native state. Such regions known as disordered regions have been shown to participate in many vital cell functions and are increasingly being examined as drug targets.
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Molecular recognition features (MoRFs) are short binding regions located in longer intrinsically disordered protein regions. Although these short regions lack a stable structure in the natural state, they readily undergo disorder-to-order transitions upon binding to their partner molecules.
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Analyzing the amino acid sequence of an intrinsically disordered protein (IDP) in an evolutionary context can yield novel insights on the functional role of disordered regions and sequence element(s).
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Proteins often contain regions that are compositionally biased (CB), i.e., they are made from a small subset of amino-acid residue types. These CB regions can be functionally important, e.g., the prion-forming and prion-like regions that are rich in asparagine and glutamine residues.
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Protein structure can be described by backbone torsion angles: rotational angles about the N-Cα bond (φ) and the Cα-C bond (ψ) or the angle between Cαi-1-Cαi -Cαi+1 (θ) and the rotational angle about the Cαi -Cαi+1 bond (τ). Thus, their accurate prediction is useful for structure prediction and model refinement.
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In the last decade and a half it has been firmly established that a large number of proteins do not adopt a well-defined (ordered) structure under physiological conditions. Such intrinsically disordered proteins (IDPs) and intrinsically disordered (protein) regions (IDRs) are involved in essential cell processes through two basic mechanisms: The entropic chain mechanism which is responsible for rapid fluctuations among many alternative conformations.
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Molecular recognition features (MoRFs) are one important type of disordered segments that can promote specific protein-protein interactions. They are located within longer intrinsically disordered regions (IDRs), and undergo disorder-to-order transitions upon binding to their interaction partners.
11p vicolorado2711 23-10-2020 22 2 Download
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Structured RNA regulatory motifs exist from the prebiotic stages of the RNA world to the more complex eukaryotic systems. In cases where a functional RNA structure is within the coding sequence a selective pressure drives a parallel co-evolution of the RNA structure and the encoded peptide domain.
16p vikuala271 13-06-2020 9 1 Download
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Adventitious rooting is an organogenic process by which roots are induced from differentiated cells other than those specified to develop roots. In forest tree species, age and maturation are barriers to adventitious root formation by stem cuttings.
19p viminato2711 22-05-2020 12 1 Download
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Dehydrins play positive roles in regulating plant abiotic stress responses. The objective of this study was to characterize two dehydrin genes, CdDHN4-L and CdDHN4-S, generated by alternative splicing of CdDHN4 in bermudagrass.
13p vishikamaru2711 29-04-2020 14 0 Download
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Baculovirus-mediated expression in insect cells is a powerful approach for protein production. However, many existing methods are time-consuming, offer limited options for protein tagging, and are unsuitable for secreted proteins requiring proteolytic maturation, such as TGF-β family growth factors.
11p vihamax2711 21-04-2020 19 2 Download
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Natively unfolded or intrinsically unstructured proteins constitute a unique group of the protein kingdom. The evolutionary persistence of such proteins represents strong evidence in the favor of their importance and raises intriguing questions about the role of protein disorders in biological processes. Additionally, natively unfolded pro-teins,withtheir lackoforderedstructure, represent attractive targets for the biophysical studies of the unfolded polypep-tidechainunderphysiological conditionsinvitro....
11p research12 29-04-2013 37 1 Download
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Proteins participate in complex sets of interactions that represent the mech-anistic foundation for much of the physiology and function of the cell. These protein–protein interactions are organized into exquisitely complex networks. The architecture of protein–protein interaction networks was recently proposed to be scale-free, with most of the proteins having only one or two connections but with relatively fewer ‘hubs’ possessing tens, hundreds or more links.
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The CII protein of bacteriophagek, which activates the synthesis of thekrepressor, plays a key role in the lysis– lysogeny switch. CII has a small in vivo half-life due to its proteolytic susceptibility, and this instability is a key com-ponent for its regulatory role. The structural basis of this instability is not known. While studying guanidine hydro-chloride-assisted unfolding of CII, we found that low concentrations of the chaotrope (50–500 mM) have a con-siderable effect on the structure of this protein.
8p fptmusic 12-04-2013 34 1 Download
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The potent immunomodulatory, anti-inflammatory and procoagulant properties of protein no. 4 secreted from the rat seminal vesicle epithelium (SV-IV) have previously been found to be modulated by a supramolecular monomer–trimer equilibrium.
12p media19 05-03-2013 35 2 Download
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Prostate apoptosis response factor-4 (Par-4) is an ubiquitously expressed pro-apoptotic and tumour suppressive protein that can both activate cell-death mechanisms and inhibit pro-survival factors. Par-4 contains a highly conserved coiled-coil region that serves as the primary recognition domain for a large number of binding partners. Par-4 is also tightly regulated by the aforementioned binding partners and by post-translational modifica-tions.
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Intrinsically disordered proteins (IDPs) are functional proteins either fully or partly lacking stable secondary and tertiary structure under physiologi-cal conditions that are involved in important biological functions, such as regulation and signalling in eukaryotes, prokaryotes and viruses.
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DNA tumor viruses ensure genome amplification by hijacking the cellular replication machinery and forcing infected cells to enter the S phase. The retinoblastoma (Rb) protein controls the G1⁄S checkpoint, and is targeted by several viral oncoproteins, among these the E7 protein from human papillomaviruses (HPVs).
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The hepatitis C virus (HCV) Core+1/S polypeptide, also known as alter-native reading frame protein (ARFP)/S, is an ARFP expressed from the Core coding region of the viral genome. Core+1/S is expressed as a result of internal initiation at AUG codons (85–87) located downstream of the polyprotein initiator codon, and corresponds to the C-terminal part of most ARFPs.
16p mobifone23 18-01-2013 29 2 Download