NMR Spectrometers: Resolution and Error Correction
¹H NMR: Interpreting Distorted and Overlapping Signals
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
¹³C NMR: Distortionless Enhancement by Polarization Transfer (DEPT)
2D NMR: Overview of Homonuclear Correlation Techniques
Other Nuclides: 31P, 19F, 15N NMR
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Updated: Apr 23, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Hyojung Ryu1, Tae-Rae Kim2, SeonJoo Ahn3
1Korean Bioinformation Center (KOBIC), Korea Research Institute of Bioscience and Biotechnology, Daejeon, The Republic of Korea; Department of Bioinformatics, University of Science and Technology, Daejeon, The Republic of Korea.
This study introduces a novel flat-bottom distance potential for refining low-quality protein structures from NMR data. The method significantly improves structural quality and secondary structure similarity, offering a more reliable approach to protein structure prediction.
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