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http://dx.doi.org/10.1038/nmat866 | DOI Listing |
Nanoscale
January 2025
Dept. of Chemical and Biomolecular Engineering, Lehigh University, Bethlehem, PA 18015, USA.
Identifying facile strategies for hierarchically structuring crystalline porous materials is critical for realizing diffusion length scales suitable for broad applications. Here, we elucidate synthesis-structure-function relations governing how room temperature catalytic conditions can be exploited to tune covalent organic framework (COF) growth and thereby access unique hierarchical morphologies without the need to introduce secondary templates or structure directing molecules. Specifically, we demonstrate how scandium triflate, an efficient catalyst involved in the synthesis of imine-based COFs, can be exploited as an effective growth modifier capable of selectively titrating terminal amines on 2D COF layers to facilitate anisotropic crystal growth.
View Article and Find Full Text PDFJ Biomol Struct Dyn
January 2025
Enzyme and Microbial Technology Research Center, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, Serdang, Selangor, Malaysia.
The quest for sustainable solutions to plastic pollution has driven research into plastic-degrading enzymes, offering promising avenues for polymer recycling applications. However, enzymes derived from natural sources often exhibit suboptimal thermostability, hindering their industrial viability. Protein engineering techniques have emerged as a powerful approach to enhance the desired properties of these biocatalysts.
View Article and Find Full Text PDFACS Catal
January 2025
Chemical Biotechnology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, 9747 AG Groningen, the Netherlands.
Aspartate ammonia lyases catalyze the reversible amination of fumarate to l-aspartate. Recent studies demonstrate that the thermostable enzyme from sp. YM55-1 (AspB) can be engineered for the enantioselective production of substituted β-amino acids.
View Article and Find Full Text PDFBrief Bioinform
November 2024
Department of Electrical Engineering and Computer Science, University of Missouri, Columbia, MO 65211, United States.
Cryo-electron microscopy (cryo-EM) has revolutionized structural biology by enabling the determination of high-resolution 3-Dimensional (3D) structures of large biological macromolecules. Protein particle picking, the process of identifying individual protein particles in cryo-EM micrographs for building protein structures, has progressed from manual and template-based methods to sophisticated artificial intelligence (AI)-driven approaches in recent years. This review critically examines the evolution and current state of cryo-EM particle picking methods, with an emphasis on the impact of AI.
View Article and Find Full Text PDFFitoterapia
January 2025
Centre for Natural Products Discovery, School of Pharmacy and Biomolecular Sciences, Liverpool John Moores University, Byrom Street, Liverpool L3 3AF, UK. Electronic address:
Infections caused by antibiotic-drug-resistant microorganisms are a major global health concern, and they result in millions of deaths every year. Methicillin-resistant Staphylococcus aureus (MRSA) is one of such drug-resistant microbial strains, and new and effective antimicrobial agents are desperately needed to combat infections caused by MRSA. In the search for effective anti-MRSA agents, the leaves of Citrus grandis (Rutaceae), also known as C.
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