Results 31 to 40 of about 1,046,387 (249)
Frontiers in Chemistry, 2019 The insertion of azobenzene moiety in complex molecular protein or peptide systems can lead to molecular switches to be used to determine kinetics of folding/unfolding properties of secondary structures, such as α-helix, β-turn, or β-hairpin. In fact, in
Francesca Nuti +14 more
doaj +1 more source
A β-barrel-like tetramer formed by a β-hairpin derived from Aβ. [PDF]
, 2023 β-Hairpins formed by the β-amyloid peptide Aβ are building blocks of Aβ oligomers. Three different alignments of β-hairpins have been observed in the structures of Aβ oligomers or fibrils.
Wierzbicki, Michał +6 more
core +1 more source
De novo ß-hairpin design using a residue-basedphysicochemical property landscape [PDF]
Structural DynamicsDe novo peptide design is a rapidly evolving field with significant promise for applications in both biological and biomedical sectors. Traditional peptide design methods often rely on sequence homology, which is limited to evolutionarily related ...
Vardhan Satalkar +2 more
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A Designed Three Stranded β-Sheet Peptide as a Multiple β-Hairpin Model
, 2016 A Designed Three Stranded β-Sheet Peptide as a Multiple β-Hairpin ...
P. Balaram (2996739) +2 more
core +1 more source
, 2013 An important nucleation event during the folding of staphylococcal nuclease involves the formation of a β-hairpin by the sequence 21DTVKLMYKGQPMTFR35.
Sasidhar, Yellamraju +5 more
core +1 more source
Computational and Structural Biotechnology Journalβ-Structure-rich amyloid fibrils are hallmarks of several diseases, including Alzheimer’s (AD), Parkinson’s (PD), and type 2 diabetes (T2D). While amyloid fibrils typically consist of parallel β-sheets, the anti-parallel β-hairpin is a structural motif ...
Laetitia F. Heid +10 more
doaj +1 more source
FEBS Letters, EarlyView.Mycobacterial 3‐methylcrotonyl‐CoA carboxylase uses a mobile biotin‐carrying domain to shuttle a carboxyl group between two catalytic sites, enabling carboxylation of 3‐methylcrotonyl‐CoA during leucine breakdown. Cryo‐electron microscopy captures the carrier at both sites and reveals an inward loop movement that may prevent futile rebinding to the ...
Ajit Yadav +2 more
wiley +1 more source
Structure-Dependent Immune Modulatory Activity of Protegrin-1 Analogs
Antibiotics, 2014 Protegrins are porcine antimicrobial peptides (AMPs) that belong to the cathelicidin family of host defense peptides. Protegrin-1 (PG-1), the most investigated member of the protegrin family, is an arginine-rich peptide consisting of 18 amino acid ...
Susu M. Zughaier +2 more
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Molecules, 2021 Cross-strand lateral ion-pairing interactions are important for antiparallel β-sheet stability. Statistical studies suggested that swapping the position of cross-strand lateral residues should not significantly affect the interaction.
Cheng-Hsin Huang +6 more
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The Shewanella oneidensis Fic enzyme SoFic targets the switch‐I region of EF‐Tu for AMPylation
FEBS Letters, EarlyView.Fic enzymes mediate diverse post‐translational modifications across all domains of life, including AMPylation. Prokaryotic EF‐Tu can be AMPylated and deAMPylated by the conserved Fic enzyme SoFic. Structural and biochemical approaches were used to characterize the effect of AMPylation on EF‐Tu, SoFic's enzymatic activities, and the enzyme‐target ...
Svenja Runge +6 more
wiley +1 more source