Results 11 to 20 of about 1,046,387 (249)
Nano-assembly of amyloid β peptide: role of the hairpin fold [PDF]
Scientific Reports, 2017 Structural investigations have revealed that β hairpin structures are common features in amyloid fibrils, suggesting that these motifs play an important role in amyloid assembly. To test this hypothesis, we characterized the effect of the hairpin fold on
Sibaprasad Maity +2 more
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The haloarchaeal MCM proteins: bioinformatic analysis and targeted mutagenesis of the β7-β8 and β9-β10 hairpin loops and conserved zinc binding domain cysteines [PDF]
Frontiers in Microbiology, 2014 The hexameric MCM complex is the catalytic core of the replicative helicase in eukaryotic and archaeal cells. Here we describe the first in vivo analysis of archaeal MCM protein structure and function relationships using the genetically tractable ...
Tatjana P Kristensen +4 more
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β-Hairpin Alignment Alters Oligomer Formation in Aβ-Derived Peptides. [PDF]
BiochemistryAmyloid-β (Aβ) forms heterogeneous oligomers, which are implicated in the pathogenesis of Alzheimer’s disease (AD). Many Aβ oligomers consist of β-hairpin building blocksAβ peptides in β-hairpin conformations.
Ruttenberg SM +3 more
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Structural relationships in the lysozyme superfamily: significant evidence for glycoside hydrolase signature motifs. [PDF]
PLoS ONE, 2010 BackgroundChitin is a polysaccharide that forms the hard, outer shell of arthropods and the cell walls of fungi and some algae. Peptidoglycan is a polymer of sugars and amino acids constituting the cell walls of most bacteria.
Alexandre Wohlkönig +3 more
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Viruses, 2021 Pestivirus envelope protein E2 is crucial to virus infection and accomplishes virus-receptor interaction during entry. However, mapping of E2 residues mediating these interactions has remained unexplored.
Fernando Merwaiss +5 more
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β-Hairpin stabilization through an interstrand triazole bridge
, 2012 β-Hairpin peptides were conformationally stabilized through a 1,4 disubstituted 1,2,3-triazole interstrand linkage. A NMR conformational analysis revealed that the β-hairpin content depends on the number and position of substituent methylene units of the
Celentano V +5 more
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Backbone N-Amination Promotes the Folding of β-Hairpin Peptides via a Network of Hydrogen Bonds. [PDF]
J Chem Inf Model, 2022 Molecular dynamics (MD) simulations have been used to characterize the effects of backbone N-amination of residues in a model β-hairpin peptide. This modification is of considerable interest as N-aminated peptides have been shown to inhibit amyloid-type ...
Dolenc J, Haywood EJ, Zhu T, Smith LJ.
europepmc +2 more sources
eLife, 2015 The eukaryotic 43S pre-initiation complex bearing tRNAiMet scans the mRNA leader for an AUG start codon in favorable context. Structural analyses revealed that the β-hairpin of 40S protein Rps5/uS7 protrudes into the 40S mRNA exit-channel, contacting the
Jyothsna Visweswaraiah +3 more
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Molecules, 2022 The β-sheet is one of the common protein secondary structures, and the aberrant aggregation of β-sheets is implicated in various neurodegenerative diseases. Cross-strand interactions are an important determinant of β-sheet stability.
Jing-Yuan Chang +8 more
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β-hairpin-mediated formation of structurally distinct multimers of neurotoxic prion peptides.
PLoS ONE, 2014 Protein misfolding disorders are associated with conformational changes in specific proteins, leading to the formation of potentially neurotoxic amyloid fibrils. During pathogenesis of prion disease, the prion protein misfolds into β-sheet rich, protease-
Andrew C Gill
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