Characterization of peptide O⋯HN hydrogen bonds via1H-detected 15N/17O solid-state NMR spectroscopy
Author:
Affiliation:
1. National High Magnetic Field Laboratory, 1800 East Paul Dirac Drive, Tallahassee, Florida, 32310, USA
2. Department of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, USA
Abstract
Funder
Division of Materials Research
National Institutes of Health
Publisher
Royal Society of Chemistry (RSC)
Subject
Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis
Link
http://pubs.rsc.org/en/content/articlepdf/2023/CC/D2CC07004A
Reference28 articles.
1. Solid-state 17O NMR studies of organic and biological molecules
2. Functional stability of water wire–carbonyl interactions in an ion channel
3. Rapid Proton-Detected NMR Assignment for Proteins with Fast Magic Angle Spinning
4. Protein resonance assignment at MAS frequencies approaching 100 kHz: a quantitative comparison of J-coupling and dipolar-coupling-based transfer methods
5. Residue-Specific High-Resolution 17O Solid-State Nuclear Magnetic Resonance of Peptides: Multidimensional Indirect 1H Detection and Magic-Angle Spinning
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1. 17O Solid-State NMR Spectroscopy of Lipid Membranes;The Journal of Physical Chemistry B;2024-04-03
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