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Study on Crack Resistance Mechanism of Helical Carbon Nanotubes in Nanocomposites.
Nanomaterials (Basel)
January 2025
Department of Architecture and Civil Engineering, City University of Hong Kong, Tat Chee Avenue, Hong Kong.
Helical carbon nanotubes (HCNTs) with different geometrical properties were constructed and incorporated into nanocomposites for the investigation of the anti-crack mechanism. The interfacial mechanical properties of the nanocomposites reinforced with straight carbon nanotubes and various types of HCNTs were investigated through the pullout of HCNTs in the crack propagation using molecular dynamics (MD). The results show that the pullout force of HCNTs is much higher than that of CNTs because the physical interlock between HCNTs and matrices is much stronger than the van der Waals (vdW) interactions between CNTs and matrices.
View Article and Find Full Text PDFStructural insights into glucose-6-phosphate recognition and hydrolysis by human G6PC1.
Proc Natl Acad Sci U S A
January 2025
Beijing National Laboratory for Condensed Matter Physics, Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China.
The glucose-6-phosphatase (G6Pase) is an integral membrane protein that catalyzes the hydrolysis of glucose-6-phosphate (G6P) in the endoplasmic reticulum lumen and plays a vital role in glucose homeostasis. Dysregulation or genetic mutations of G6Pase are associated with diabetes and glycogen storage disease 1a (GSD-1a). Studies have characterized the biophysical and biochemical properties of G6Pase; however, the structure and substrate recognition mechanism of G6Pase remain unclear.
View Article and Find Full Text PDFBackbone Hydration of -Helical Peptides: Hydrogen-Bonding and Surface Hydrophobicity/Hydrophilicity.
Mol Phys
March 2024
Department of Physics, Brooklyn College of the City University of New York, Brooklyn, NY 11210, United States.
The stability of proteins and small peptides depends on the way they interact with the surrounding water molecules. For small peptides, such as -helical polyalanine (polyALA), water molecules can weaken the intramolecular hydrogen-bonds (HB) formed between the peptide backbone O and NH groups which are responsible for the -helix structure. Here, we perform molecular dynamics simulations to study the hydration of polyALA, polyserine (polySER), and other homopolymer peptide -helices at different temperatures and pressures.
View Article and Find Full Text PDFStructure and Function Analysis of Microcystin Transport Protein MlrD.
Biochimie
January 2025
School of Chemistry and Biological Engineering, University of Science and Technology Beijing, Beijing, 100083, China. Electronic address:
Microorganisms play a crucial role in the degradation of microcystins (MCs), with most MC-degrading bacteria utilizing the mlr gene cluster (mlrABCD) mechanism. While previous studies have advanced our understanding of the structure, function, and degradation mechanisms of MlrA, MlrB, and MlrC, research on MlrD remains limited. Consequently, the molecular structure and specific catalytic processes of MlrD are still unclear.
View Article and Find Full Text PDFStructural and functional analysis of the Nipah virus polymerase complex.
Cell
January 2025
Department of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA; Department of Medicine, Division of Infectious Diseases, Brigham & Women's Hospital, Boston, MA, USA; Center for Integrated Solutions in Infectious Diseases, Broad Institute of Harvard and MIT, Cambridge, MA, USA; Howard Hughes Medical Institute, Boston, MA, USA. Electronic address:
Nipah virus (NiV) is a bat-borne, zoonotic RNA virus that is highly pathogenic in humans. The NiV polymerase, which mediates viral genome replication and mRNA transcription, is a promising drug target. We determined the cryoelectron microscopy (cryo-EM) structure of the NiV polymerase complex, comprising the large protein (L) and phosphoprotein (P), and performed structural, biophysical, and in-depth functional analyses of the NiV polymerase.
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