The editors of this special volume suggested this topic, presumably because of the perspective lent by our combined >90-year association with biomolecular NMR. What follows is our personal experience with the evolution of the field, which we hope will illustrate the trajectory of change over the years. As for the future, one can confidently predict that it will involve unexpected advances. Our narrative is colored by our experience in using the NMR Facility for Biomedical Studies at Carnegie-Mellon University (Pittsburgh) and in developing similar facilities at Purdue (1977-1984) and the University of Wisconsin-Madison (1984-). We have enjoyed developing NMR technology and making it available to collaborators and users of these facilities. Our group's association with the Biological Magnetic Resonance data Bank (BMRB) and with the Worldwide Protein Data Bank (wwPDB) has also been rewarding. Of course, many groups contributed to the early growth and development of biomolecular NMR, and our brief personal account certainly omits many important milestones.
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http://dx.doi.org/10.1016/j.abb.2017.05.003 | DOI Listing |
ACS Nano
January 2025
Department of Chemical and Biomolecular Engineering, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.
Ordered nanoporous polymer membranes offer opportunities for systematically probing the mechanisms of ion transport under confinement and for realizing useful materials for electrochemical devices. Here, we examine the impact of morphology and ion hydration on the transport of hydroxide and bromide anions in nanostructured polymer membranes with 1 nm scale pores. We use aqueous lyotropic self-assembly of an amphiphilic monomer, with a polymerizable surfactant to create direct hexagonal (H) and gyroid mesophases.
View Article and Find Full Text PDFPhys Chem Chem Phys
January 2025
Magnetic Resonance Center (CERM), University of Florence, via Luigi Sacconi 6, Sesto Fiorentino, 50019, Italy.
The function of biomolecular systems, including biological macromolecules, often crucially depends on their dynamics. Nuclear magnetic resonance (NMR) is one of the most informative methods used to study biomolecules and their internal mobility, with atomic resolution, in near-physiological conditions. NMR relaxation profiles, obtained from the field dependence of the nuclear relaxation rates, in particular, offer the possibility to probe dynamic processes over a wide range of time scales.
View Article and Find Full Text PDFCurr Protoc
January 2025
Czech Metrology Institute, Brno, Czech Republic.
Atomic force microscopy (AFM) has recently received increasing interest in molecular biology. This technique allows quick and reliable detection of biomolecules. However, studying RNA-protein complexes using AFM poses significant challenges.
View Article and Find Full Text PDFPhytochem Anal
January 2025
Department of Natural Drugs, Faculty of Pharmacy, Masaryk University, Brno, Czech Republic.
Introduction: Ziziphora clinopodioides subsp. bungeana (Juz.) Rech.
View Article and Find Full Text PDFActa Crystallogr E Crystallogr Commun
January 2025
Department of Chemistry, KU Leuven, Biomolecular Architecture, Celestijnenlaan 200F, Leuven (Heverlee), B-3001, Belgium.
Two novel complexes, [Cu()Cl] and [Zn()Cl], were synthesized from 1,1'-[(3-fluoro-phen-yl)methyl-ene]bis-[3-(3-fluoro-phen-yl)imidazo[1,5-]pyridine] (), and copper(II) and zinc(II) chloride, respectively. The structures of these complexes were confirmed using ESI-MS, IR and H NMR spectra. The results reveal mononuclear structures in which the central metal atoms are coordinated by two N atoms from the imidazole rings and two Cl ligands.
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