• For example, amyloid beta is a major component of amyloid plaques in the brains of Alzheimer's disease patients, and polyglutamine repeats in the huntingtin protein are associated with Huntington's disease. (wikipedia.org)
  • Protein misfolding and aggregation are common pathological features of several human diseases, including Alzheimer's disease and type 2 diabetes. (nature.com)
  • We demonstrate the effectiveness of this approach by identifying drug-like, head-to-tail cyclic peptides that modulate the aggregation of the Alzheimer's disease-associated amyloid β peptide. (nature.com)
  • Biochemical, biophysical and biological assays using isolated amyloid β peptide, primary neurons and various established Alzheimer's disease nematode models showed that the selected macrocycles potently inhibit the formation of neurotoxic amyloid β peptide aggregates. (nature.com)
  • β-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer's therapy. (nature.com)
  • Aggregation of β-amyloid (Aβ) peptide is one of the hallmarks of Alzheimer's disease (AD) which results in chronic and progressive neurodegeneration of the brain. (ncbs.res.in)
  • Alzheimer's disease (AD), the most common form of dementia, is characterized by the accumulation of amyloid β (Aβ) and hyperphosphorylated tau protein aggregates. (biomedcentral.com)
  • Kaniyappan S , Balaji V, Wang Y, Mandelkow E . Microfluidic Chamber Technology to Study Missorting and Spreading of Tau Protein in Alzheimer's Disease. (neurotree.org)
  • Wegmann S , Biernat J, Mandelkow E . A current view on Tau protein phosphorylation in Alzheimer's disease. (neurotree.org)
  • Their research is focused on the development of new treatments for diseases caused by protein aggregation, including Alzheimer's disease and transthyretin amyloidosis. (researchoutreach.org)
  • We use both top-down and bottom-up approaches to explore the aggregation of the Aβ peptide involved in Alzheimer's disease. (lu.se)
  • Oligomers of Aβ peptide are implicated as the most probable causative agent in Alzheimer's disease. (nature.com)
  • However recent evidence suggests that macroscopic aggregates are an attempt from the cell to sequester aberrant proteins while soluble (micro-) oligomers of such proteins are the most harmful forms [23]. (buyresearchchemicalss.net)
  • Oligomers are toxic in an array of protein misfolding and aggregation (PMA) disorders. (neurodegenerationresearch.eu)
  • Amyloid fibrils are made of normally soluble misfolded proteins that aggregate into oligomers and then insoluble fibrils. (msdmanuals.com)
  • However, some prefibrillar oligomers of amyloidogenic proteins have direct cellular toxicity, an important component of disease pathogenesis. (msdmanuals.com)
  • neurotoxic PrPC mutants generate a smaller complex that is uncleaved. (neurodegenerationresearch.eu)
  • A novel D-amino acid peptide with therapeutic potential (ISAD1) inhibits aggregation of neurotoxic disease-relevant mutant Tau and prevents Tau toxicity in vitro. (neurotree.org)
  • The alpha sheet has been proposed as a possible intermediate state in the conformational change in the formation of amyloid fibrils by peptides and proteins such as amyloid beta, poly-glutamine repeats, lysozyme, prion proteins, and transthyretin repeats, all of which are associated with protein misfolding disease. (wikipedia.org)
  • These proteins undergo a conformational change from largely random coil or alpha helix structures to the highly ordered beta sheet structures found in amyloid fibrils. (wikipedia.org)
  • UVRR enables monitoring of the protein and peptide conformational distributions and Gibbs free energy landscapes along the Ramachandran Ψ coordinate. (pitt.edu)
  • We also measured UVRR spectra of Leu26 deuterated peptides to determine conformational distributions of Leu26 in the p53 peptides. (pitt.edu)
  • In heterozygotes, then, the single mutant allele may actually protect against Alzheimer disease by preventing stable Aβ aggregates from forming, Tagliavini said. (alzforum.org)
  • Notch3-ECD-containing aggregates are the earliest manifestation of the disease and excess Notch3-ECD is believed to recruit functionally important extracellular matrix proteins resulting in brain vessel dysfunction. (uni-muenchen.de)
  • Cell culture studies revealed that IGF2 treatment decreases the load of intracellular aggregates of mutant huntingtin and a polyglutamine peptide. (uchile.cl)
  • Amyloidosis results from the accumulation of pathogenic amyloids-most of which are aggregates of misfolded proteins-in a variety of tissues. (medscape.com)
  • Our current findings provide novel structural insights on the mode of interaction between cyclotides and Aβ fibrils and describe their anti-amyloid aggregation potential. (ncbs.res.in)
  • In this review we describe some structural properties of α-synuclein and the two mutant forms, as well as α-synuclein fragments, with particular emphasis on their ability to form β-sheet on ageing and aggregate to form amyloid-like fibrils. (uaeu.ac.ae)
  • Differences in the rates of aggregation and morphologies of the fibrils formed by α-synuclein and the two mutant proteins are high-lighted. (uaeu.ac.ae)
  • El-Agnaf, OMA & Irvine, GB 2000, ' Review: Formation and properties of amyloid-like fibrils derived from α-synuclein and related proteins ', Journal of Structural Biology , vol. 130, no. 2-3, pp. 300-309. (uaeu.ac.ae)
  • Amyloid fibrils are protein polymers comprising identical monomer units (homopolymers). (medscape.com)
  • [ 5 ] Only 10% of amyloidosis deposits consist of components such as glycosaminoglycans (GAGs), apolipoprotein-E (apoE), and serum amyloid P-component (SAP), while nearly 90% of the deposits consist of amyloid fibrils that are formed by the aggregation of misfolded proteins. (medscape.com)
  • [ 6 ] In humans, about 23 different unrelated proteins are known to form amyloid fibrils in vivo. (medscape.com)
  • Amyloidosis is a group of rare but serious conditions caused when deposits of damaged proteins known as amyloid fibrils, accumulate around tissues and organs. (researchoutreach.org)
  • This structural change leads to the protein aggregation and the creation of the amyloid fibrils. (researchoutreach.org)
  • Amyloidosis is any of a group of disparate conditions characterized by extracellular deposition of insoluble fibrils composed of misaggregated proteins. (msdmanuals.com)
  • Antimicrobial proteins and peptides offer a multifaceted mechanism suitable to fight bacterial resistance. (frontiersin.org)
  • The inhibition of one of these steps by small molecules, such as antimicrobial peptides, or their action on specific targets will leave pathogens armless against classical antibiotics. (intechopen.com)
  • Inhibition of Tau aggregation with BSc3094 reduces Tau and decreases cognitive deficits in rTg4510 mice. (neurotree.org)
  • Targeting soluble Aβ peptide with Tramiprosate for the treatment of brain amyloidosis. (nature.com)
  • Cardiac amyloidosis, which is commonly caused by aggregation of immunoglobulin light chain (AL) or transthyretin (TTR), is a main contributor of morbidity and mortality in patients with amyloidosis. (researchoutreach.org)
  • TTR amyloidosis (ATTR) is a progressive, fatal disease in which deposition of amyloid derived from either mutant or wild-type TTR causes severe organ damage and dysfunction. (researchoutreach.org)
  • A number of normal (wild-type) and mutant proteins are susceptible to such misfolding and aggregation (amyloidogenic proteins), thus accounting for the wide variety of causes and types of amyloidosis. (msdmanuals.com)
  • For amyloidosis to develop, in addition to production of amyloidogenic proteins, there is probably also a failure of the normal clearance mechanisms for such misfolded proteins. (msdmanuals.com)
  • In systemic amyloidosis, circulating amyloidogenic proteins form deposits in a variety of organs. (msdmanuals.com)
  • Amyloidosis caused by aggregation of beta-2-microglobulin can occur in patients on long-term hemodialysis, but the incidence has declined with use of modern high-flow dialysis membranes. (msdmanuals.com)
  • Localized forms of amyloidosis appear to be caused by local production and deposition of an amyloidogenic protein (most often immunoglobulin light chains) within the affected organ rather than by deposition of circulating proteins. (msdmanuals.com)
  • Fig. 4: The selected cyclic pentapeptides AβC5-34 and AβC5-116 inhibit Aβ-induced aggregation and cytotoxicity in vivo. (nature.com)
  • We previously reported the in vivo modeling of a clinical surfactant protein C (SP-C) mutation that led to AEC2 endoplasmic reticulum (ER) stress and spontaneous lung fibrosis, providing proof of concept for disruption to proteostasis as a proximal driver of PF. (bvsalud.org)
  • However, peptide aggregation in vivo typically occurs in a more complex environment, surrounded by either different proteins or lipids, or both. (lu.se)
  • The regular formation of alpha-sheet by unfolded proteins inevitably involves many L amino acid residues readily adopting the alphaL conformation, which appears at first sight to go against textbook chemistry, which is that, of the 20 amino acids, it is glycine that strongly favours this conformation. (wikipedia.org)
  • One of the conserved hydrophobic interface residues, Tyr10 was mutated to Ala and the impact of this virtual mutation was estimated by additional MD simulations for the wild-type (WT) and mutant protein-peptide complexes. (ncbs.res.in)
  • In Chapter 6, we reported the first time experimental measurements of Ramachandran Ψ-angle distributions for intrinsically disordered peptides: the N-terminal peptide fragment (Residues 17-29) of tumor suppressor p53 and its P27S mutant form. (pitt.edu)
  • A molecular model of the FMDV 3A protein, derived from the nuclear magnetic resonance (NMR) structure of the poliovirus 3A protein, predicted a hydrophobic interface spanning residues 25 to 44 as the main determinant for 3A dimerization. (asm.org)
  • Replacements L38E and L41E, involving charge acquisition at residues predicted to contribute to the hydrophobic interface, reduced the dimerization signal in the protein ligation assay and prevented the detection of dimer/multimer species in both transiently expressed 3A proteins and in synthetic peptides reproducing the N terminus of 3A. (asm.org)
  • We found that the C-terminal domain of DNAJB6 - suggested to be involved in peptide binding after dimerization - will inhibit the secondary nucleation of Aβ fibril formation as opposed to the intact protein which inhibits the primary nucleation. (lu.se)
  • In the late 1990s, she pioneered the use of engineered antibody fragments (nanobodies and intrabodies) to counteract the cellular effects of misfolded proteins in stressed and aging cells. (neuralsci.org)
  • Biochemical and histological approaches on post-mortem brain tissue from CADASIL patients and control subjects as well as in vitro assays were used to study the consequences of Notch3-ECD deposition on the ECM components thrombospondin-2, fibrillin-1 and fibronectin and members of the latent transforming growth factor-β (TGF-β) binding protein (LTBP) family. (uni-muenchen.de)
  • Finally, a direct interaction of LTBP-1 with Notch3-ECD is demonstrated and evidence for a co aggregation with mutant Notch3 in vitro is provided. (uni-muenchen.de)
  • Hochmair J, Exner C, Betzel C, Mandelkow E , Wegmann S . Light Microscopy and Dynamic Light Scattering to Study Liquid-Liquid Phase Separation of Tau Proteins In Vitro. (neurotree.org)
  • Combining in vitro studies with studies in cell models, we found that this mutation reduces aSyn aggregation and increases proteasome activity, altering normal proteostasis. (biomedcentral.com)
  • Humanin (HN) is a short bioactive peptide abolishing neuronal cell death induced by various familial AD (FAD)-causative genes and amyloid-β (Aβ) in vitro . (jneurosci.org)
  • Scientists have discovered a recessive mutation in β amyloid precursor protein that causes early onset Alzheimer disease in two siblings from a small south Italian village. (alzforum.org)
  • We observed that, in our experimental paradigms, the A53E mutation affects specific steps of the aggregation process of aSyn and different cellular processes, providing novel ideas about the molecular mechanisms involved in synucleinopathies. (biomedcentral.com)
  • Amond them, the A21G Flemish mutation is unique as it shows a low tendency to aggregation, while deposits progressively appear in the vessel walls. (anaspec.com)
  • Dr. Messer pioneered adapting this technology to target the expanded polyglutamine (polyQ) region of mutant huntington (mHTT) intracellularly, which opened up the entire field of antibody engineering for neurodegenerative diseases. (neuralsci.org)
  • The lining of the alveoli is covered by pulmonary surfactant, a complex mixture of surface-active lipids and proteins that enables efficient gas exchange between inhaled air and the circulation. (bvsalud.org)
  • Despite decades of advancements in the study of the pulmonary surfactant, the molecular scale behavior of the surfactant and the inherent role of the number of different lipids and proteins in surfactant behavior are not fully understood. (bvsalud.org)
  • The research done contributes to a better understanding of the roles of specific lipids and proteins in surfactant function, thus helping to develop better synthetic products for surfactant replacement therapy used in the treatment of many fatal lung-related injuries and diseases. (bvsalud.org)
  • Additional studies have revealed a potential mechanism of action of anti-Aβ antibodies via experiments on transgenic mice overexpressing mutant human amyloid precursor protein (PDAPP) under the control of the mini-promoter of platelet-derived growth factor (PDGF) [ 9 ]. (biomedcentral.com)
  • Overexpression of wild-type human amyloid precursor protein alters GABAergic transmission. (uclouvain.be)
  • In this review, we assess the potential role of putative gut microbiota products in the etiopathogeny of Parkinson's disease, with a special emphasis on functional bacterial amyloid proteins, bacterial biosurfactants, endotoxins and short-chain fatty acids. (techscience.com)
  • abstract = "Synucleins are small proteins that are highly expressed in brain tissue and are localised at presynaptic terminals in neurons. (uaeu.ac.ae)
  • It is found in the serum and the cerebrospinal fluid and named after its function in transporting thyroxine and retinol (vitamin A). TTR is coded for by the TTR gene, and a faulty copy of this gene can lead to misfolding of the TTR protein. (researchoutreach.org)
  • Impaired elimination and accumulation of soluble and insoluble β-amyloid peptide may underlie the pathogenesis of CAA and explain the link between CAA and Alzheimer disease (AD). (medscape.com)
  • Although the alpha sheet is only rarely observed in natural protein structures, it has been speculated to play a role in amyloid disease and it was found to be a stable form for amyloidogenic proteins in molecular dynamics simulations. (wikipedia.org)
  • 5 S-Nitrosylation of Parkin and the UPS Studies of rare mutations have exposed key components of the mechanism for protein aggregation and pathology in PD including sporadic forms of the disease. (buyresearchchemicalss.net)
  • Using synthetic peptides and laser light scattering to measure clumping, they found that the mutant peptide aggregated faster than wild-type. (alzforum.org)
  • Using wild-type and mutant synthetic peptides, we demonstrate that the hydrophobicity of this domain is required for the aggregation and the lipid mixing of phospholipid vesicles, supporting the role of TM1 as the fusion peptide. (edu.au)
  • The reduction in the levels of mutant huntingtin was associated with a decrease in the half-life of the intracellular protein. (uchile.cl)
  • α-Synuclein has been identified as a component of intracellular fibrillar protein deposits in several neurodegenerative diseases, and two mutant forms of α-synuclein have been associated with autosomal-dominant Parkinson's Disease. (uaeu.ac.ae)
  • We observed the proteins internalization within macrophages and their capacity to eradicate the intracellular mycobacterial infection at a low micro-molar range. (frontiersin.org)
  • Two well-defined pathological hallmarks of AD have been described: the formation of extracellular amyloid plaques and the development of intracellular neurofibrillary tangles (NFTs) formed by aggregated hyperphosphorylated TAU protein [ 4 ]. (biomedcentral.com)
  • Intracellular misfolding and abnormal accumulation of a neuronal protein are the triggering events in many neurodegenerative diseases including Huntington's disease and Parkinson's disease. (neuralsci.org)
  • The exact function of aSyn remains unclear, but it is known to be associated with vesicles and membranes, and to have an impact on important cellular functions such as intracellular trafficking and protein degradation systems, leading to cellular pathologies that can be readily studied in cell-based models. (biomedcentral.com)
  • NS proteins are involved in crucial aspects of the viral cycle and pathogenesis, such as rearrangements of intracellular membranes required for endomembrane recruitment and the lysis of host cells ( 1 , 12 , 14 , 18 , 73 ). (asm.org)
  • in poliovirus (PV), the interaction between the RNA replication complex and intracellular membranes appears to be accomplished by proteins 3A and 2C, which have membrane-binding properties ( 11 , 60 ). (asm.org)
  • When expressed as a recombinant protein in transfected cells, PV 3A cofractionates with endoplasmic reticulum markers ( 66 ), and its single transient expression can disrupt the secretory apparatus ( 23 ) and decrease major histocompatibility complex (MHC) class I expression ( 22 ). (asm.org)
  • Additionally, we detected increased levels of active glycogen synthase kinase 3 β, a physiological kinase of TAU, in neurons derived from AD iPSCs, as well as significant upregulation of amyloid precursor protein (APP) synthesis and APP carboxy-terminal fragment cleavage. (biomedcentral.com)
  • This sheds light on the future of cyclotide-based drug design against protein aggregation, a hallmark event in many neurodegenerative diseases. (ncbs.res.in)
  • The toxicity of α-synuclein and related peptides towards neurons is also discussing in relation to the aetiology of neurodegenerative diseases. (uaeu.ac.ae)
  • A hydrophobic domain in the large envelope protein is essential for fusion of duck hepatitis B virus. (edu.au)
  • Fig. 7: Genetic screening and identification of cyclic oligopeptides that rescue the misfolding and aggregation of mutant SOD1. (nature.com)
  • Palmitoylation of superoxide dismutase 1 (SOD1) is increased for familial amyotrophic lateral sclerosis-linked SOD1 mutants. (chicagobiomedicalconsortium.org)
  • Dr. Messer applied her expertise from the Huntington's disease project to a series of other projects including engineering antibody fragments as intrabodies against α-Syn, a protein that is critical to the onset of Parkinson's disease. (neuralsci.org)
  • we identified a novel gene encoding a 24 amino acid peptide named Humanin (HN) that suppressed neuronal death induced by any type of FAD genes thus far examined, toxic Aβ peptides, and anti-APP antibody (Hashimoto et al. (jneurosci.org)
  • Interactions between α-synuclein and other proteins, especially those that are components of amyloid or Lewy bodies, are considered. (uaeu.ac.ae)
  • In agreement with previous research, the inclusion of either SP-B and SP-C increases surface pressure, and our simulations provide a molecular scale explanation for this effect: The proteins display preferential lipid interactions with phosphatidylglycerol, they reside predominantly in the lipid acyl chain region, and they partition into the liquid expanded phase or even induce it in an otherwise packed monolayer. (bvsalud.org)
  • Native or wild-type quaternary protein structure is usually born from a single translated protein sequence with one ordered conformation with downstream protein interactions. (medscape.com)
  • He heads a multi-disciplinary team working in the field of protein-protein interactions. (researchoutreach.org)
  • the amyloidogenic protein is typed using a variety of immunohistologic and biochemical techniques. (msdmanuals.com)
  • This leads to the abnormal multimerization and extracellular deposition of mutant Notch3-ECD at the plasma membrane of smooth muscle cells in small blood vessels. (uni-muenchen.de)
  • Polymorphisms that slightly vary native peptides or inflammatory processes set the stage for abnormal protein folding and amyloid fibril deposition. (medscape.com)
  • These proteins either arise from proteins expressed by cells at the deposition site (localized), or they precipitate systemically after production at a local site (systemic). (medscape.com)
  • 2005. Protection by dietary zinc in ALS mutant G93A SOD transgenic mice. . (oregonstate.edu)
  • Di Fede and colleagues then turned to biochemistry to assay the mutation's effects on aggregation. (alzforum.org)
  • In this system, large combinatorial libraries of macrocyclic molecules are biosynthesized in Escherichia coli cells and simultaneously screened for their ability to rescue pathogenic protein misfolding and aggregation using a flow cytometric assay. (nature.com)
  • In this work, FMDV 3A homodimerization was evidenced by an in situ protein fluorescent ligation assay. (asm.org)
  • The most important proteins in this complex system are the surfactant proteins SP-B and SP-C. Given this, in this work we performed nonequilibrium all-atom molecular dynamics simulations to study the interplay of SP-B and SP-C with multicomponent lipid monolayers mimicking the pulmonary surfactant in composition. (bvsalud.org)
  • Xu, using atomic force microscopy, has shown that formation of amyloid fibers is a two-step process in which proteins first aggregate into colloidal spheres of ≈20 nm diameter. (wikipedia.org)
  • Fig. 1: High-throughput genetic screening for the discovery of macrocyclic rescuers of pathogenic Aβ misfolding and aggregation. (nature.com)
  • Aggregated proteins were 1st considered to be pathogenic. (buyresearchchemicalss.net)
  • It is now well established that the aggregation and spread of alpha-synuclein aggregation pathology activate numerous pathogenic mechanisms that contribute to neurodegeneration and, ultimately, to disease progression. (mdpi.com)
  • This study identifies IGF2 as a relevant factor deregulated in HD, operating as a disease modifier that buffers the accumulation of abnormal protein species. (uchile.cl)
  • Moreover, the accumulation of aSyn in Lewy Bodies and Lewy neurites in disorders such as PD, dementia with Lewy bodies, or multiple system atrophy, suggests aSyn misfolding and aggregation plays an important role in these disorders, collectively known as synucleinopathies. (biomedcentral.com)
  • The accumulation of the various products of alpha-synuclein aggregation has been associated with the etiology and pathogenesis of several neurodegenerative conditions, including both familial and sporadic forms of Parkinson's disease (PD) and dementia with Lewy bodies (DLB). (mdpi.com)
  • Formation of polyubiquitin chains on a peptide constitutes JWH 073 the transmission for proteasomal degradation. (buyresearchchemicalss.net)
  • Functional amyloids play a beneficial role in a variety of physiologic processes (eg, long-term memory formation, gradual release of stored peptide hormones). (medscape.com)
  • In this section, we will focus on proteins involved in biofilm formation as useful targets for the development of new drugs that can effectively and specifically impair biofilm formation with slight effects on cell survival, thus avoiding the generation of drug-resistant strains. (intechopen.com)
  • Administration of IGF2 into the brain of HD mice using gene therapy led to a significant decrease in the levels of mutant huntingtin in three different animal models. (uchile.cl)
  • Mutations in the surfactant protein C gene (SFTPC) are responsible for hereditary interstitial lung disease (ILD), which is a rare disease. (bvsalud.org)
  • We will perform genome-wide analysis of DNA methylation in blood from 2000 adolescents part of the IMAGEN study on factors that influence mental health in adolescents ( http://www.imagen-europe.com/en/the-imagen-study.php ), and of genotype, DNA methylation and gene expression in brain from circa 400 controls at different developmental stages and adult alcohol dependents. (uu.se)
  • Center Groningen, The Netherlands, we have identified missense mutations in the human prodynorphin gene ( PDYN ) coding for a precursor to opioid peptides dynorphins (Bakalkin et al. (uu.se)
  • Deposited amyloid protein in these patients is identical to the amyloid protein seen in sporadic cases, and the likely genetic defect is in the amyloid protein precursor protein ( APP ) gene on chromosome 21. (medscape.com)
  • The viral genome encodes four structural capsid proteins (VP1 to VP4) and seven nonstructural (NS) proteins, the leader Lb/ab protease, and proteins encoded in the P2 (2B and 2C) and P3 (3A, 3B, 3C, and 3D) regions ( 9 ). (asm.org)
  • We also applied the system to the identification of misfolding rescuers of mutant Cu/Zn superoxide dismutase-an enzyme linked with inherited forms of amyotrophic lateral sclerosis. (nature.com)
  • 2004. Aggregation of ALS mutant superoxide dismutase expressed in Escherichia coli. . (oregonstate.edu)
  • Conversely, IGF2 signaling enhanced the secretion of soluble mutant huntingtin species through exosomes and microvesicles involving changes in actin dynamics. (uchile.cl)
  • We utilized UVRR to examine the dependence of Gibbs free energy landscapes of an α-helical peptide on solution environment such as salt species (Chapter 3) and alcohol species (Chapter 4). (pitt.edu)
  • Evidence for the existence of alpha-sheet in a mutant form of transthyretin has been presented. (wikipedia.org)
  • Here, we studied the impact of IGF2 signaling on protein aggregation in models of Huntington's disease (HD) as proof of concept. (uchile.cl)
  • Lecerf, J.M., T.L. Shirley, Q. Zhu, A. Kazantsev, P. Amersdorfer, D.E. Housman, A. Messer , and J.S. Huston (2001) Human single- chain Fv intrabodies counteract in situ huntingtin aggregation in cellular models of Huntington's Disease. (neuralsci.org)
  • Western blot analysis of HD brain tissue shows full-length huntingtin protein in the nuclear fraction as well as abundant immunopositive bands at lower molecular weight, suggesting proteolytic products in the nucleus. (jci.org)
  • While lipid mixing occurred at pH 7, the kinetics of insertion of the fusion peptide was increased at pH 5, consistent with the location of DHBV in the late-endosome compartment and previous studies of the nonessential role of low pH for infectivity. (edu.au)
  • The kinetics of misfolding can be altered by changing the protein context of the initiating peptides in these proteins. (neuralsci.org)
  • Native proteins containing alpha-strand regions or alpha-sheet-patterned hydrogen bonding include synaptotagmin, lysozyme, and potassium channels, where the alpha-strands line the ion-conducting pore. (wikipedia.org)
  • A detailed MD simulation analyses revealed that cyclotides form hydrogen bonds with the toxic amyloid assemblies thereby weakening the inter-strand hydrogen bonds between the Aβ peptide. (ncbs.res.in)
  • In Chapter 8, we developed a method and for the first time directly monitored the backbone and side chain hydrogen bonding of a polyGLN peptide whose solution structure can be controlled to either fibrillize or not fibrillize. (pitt.edu)
  • Alpha sheet (also known as alpha pleated sheet or polar pleated sheet) is an atypical secondary structure in proteins, first proposed by Linus Pauling and Robert Corey in 1951. (wikipedia.org)
  • Secondary-structure predictions indicate that L and S have three alpha-helical, membrane-spanning domains, with TM1 predicted to act as the fusion peptide following endocytosis of DHBV into the hepatocyte. (edu.au)
  • UV resonance Raman spectroscopy (UVRR) is the most useful dilute solution method to quickly determine protein and peptide secondary structure. (pitt.edu)
  • The cascade of JWH 073 activation (E1) conjugation (E2) and ubiquitin-ligase (E3)-type enzymes catalyzes the conjugation of the ubiquitin chain to the proteins designated for degradation. (buyresearchchemicalss.net)
  • Their current work in peptide conjugation is showing great promise. (researchoutreach.org)
  • Protein Expression and Purification. (lu.se)