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Revealing the mechanism underlying the viscosity improvement of rice protein yogurt by the presence of in-situ-produced dextrans.
Int J Biol Macromol
January 2025
College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei Province 430070, PR China. Electronic address:
The in-situ-produced dextrans (DXs) could effectively enhance the viscosity of rice protein (RP) yogurt, but the reason for this improvement has not been elucidated. This study aims to reveal the mechanism underlying the viscosity improvement of RP yogurt by the presence of in-situ DXs. DXs synthesized in RP yogurts under different optimum conditions were purified and fully characterized.
View Article and Find Full Text PDFExploring the Effect of Hydrocarbon Cross-Linkers on the Structure and Binding of Stapled p53 Peptides.
Proteins
January 2025
Department of Chemistry, Indian Institute of Technology Bombay, Mumbai, India.
Short-length peptides are used as therapeutics due to their high target specificity and low toxicity; for example, peptides are designed for targeting the interaction between oncogenic protein p53 and E3 ubiquitin ligase MDM2. These peptide therapeutics form a class of successful inhibitors. To design such peptide-based inhibitors, stapling is one of the methods in which amino acid side chains are stitched together to get conformationally rigid peptides, ensuring effective binding to their partners.
View Article and Find Full Text PDFElectronic Polarizability Tunes the Function of the Human Bestrophin 1 Cl Channel.
J Chem Theory Comput
January 2025
Department of Physics, Clarendon Laboratory, University of Oxford, Oxford OX1 3PU, U.K.
Mechanisms of anion permeation within ion channels and nanopores remain poorly understood. Recent cryo-electron microscopy structures of the human bestrophin 1 Cl channel (hBest1) provide an opportunity to evaluate ion interactions predicted by molecular dynamics (MD) simulations against experimental observations. Here, we implement the fully polarizable force field AMOEBA in MD simulations on different conformations of hBest1.
View Article and Find Full Text PDFThe structure of FCGBP is formed as a disulfide-mediated homodimer between its C-terminal domains.
FEBS J
January 2025
Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, University of Gothenburg, Sweden.
Mucus in the colon is crucial for intestinal homeostasis by forming a barrier that separates microbes from the epithelium. This is achieved by the structural arrangement of the major mucus proteins, such as MUC2 and FCGBP, both of which are comprised of several von Willebrand D domains (vWD) and assemblies. Numerous disulfide bonds stabilise these domains, and intermolecular bonds generate multimers of MUC2.
View Article and Find Full Text PDFTRAMP assembly alters the conformation and RNA binding of Mtr4 and Trf4-Air2.
Proc Natl Acad Sci U S A
January 2025
Department of Chemistry and Biochemistry, The University of Texas at Dallas, Richardson, TX 75080.
Article Synopsis
- The TRAMP complex is crucial for RNA processing and features two key enzymatic activities that involve both polyadenylation and unwinding of RNA.
- New research using hydrogen-deuterium exchange data reveals insights into how TRAMP assembles and shuffles RNA between its catalytic sites, which are not fully understood.
- Findings indicate that peripheral RNA-recognition motifs affect TRAMP assembly and that different active-site subunits interact with tRNA in ways that influence RNA transfer between TRAMP components.
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