Application of Nuclear Magnetic Resonance Method in Protein Research
A special issue of Life (ISSN 2075-1729). This special issue belongs to the section "Proteins and Proteomics".
Deadline for manuscript submissions: closed (31 August 2022) | Viewed by 9543
Special Issue Editors
Interests: solid-state NMR; protein structure; conformational dynamics; membrane protein; ion channel; intramembrane protease; transporter
Interests: NMR; protein structure and dynamics; protein folding; protein–protein interactions; antibody and nanobody; membrane protein; chaperones
Interests: NMR; structure biology; high-throughput screening; protein–ligand interaction; virus protein structure
Special Issue Information
Dear Colleagues,
Nuclear magnetic resonance (NMR) is one of the three major methods used to study protein structure at an atomic resolution. Recently, there has been a revolution in structural biology involving cryogenic-electron microscopy. However, the molecular mechanisms and biological roles for most proteins could not be perfectly illustrated with these frozen static structures. In addition to its high-resolution structure, NMR enables the studies of protein dynamics under the more physiological conditions intimately related to the biological mechanism of proteins. With special labeling schemes and advanced data acquisition methods, the size limit of protein solution NMR studies has been largely extended. In the last decade, magic angle spinning (MAS) solid-state NMR has been successfully used in protein studies due to the ultra-fast spinning and new detection methodology development. Because it is no longer limited by molecular size or lack of long-range order, NMR may be a promising technique for protein studies in complex biological environments, such as protein in lipid membranes, in cells or large biomolecular complexes spanning from well-defined protein complexes to highly dynamical membrane-less organelles. Additionally, NMR is used extensively in drug discovery, such as in high-throughput screening and protein–ligand interaction.
This Special Issue aims to highlight recent advances in all aspects of NMR-based protein study methodology and applications. It shall broadly contain reviews and original scientific contributions, including solution and solid-state NMR pulse sequence development, data analysis, as well as domain-specific applications such as protein structure determinations, drug discovery, chemical biology, and protein biological function investigations. Submissions of original research articles, short communications, perspectives, and comprehensive review articles are all welcome.
Prof. Dr. Chaowei Shi
Prof. Dr. Lichun He
Prof. Dr. Yan Li
Prof. Dr. Bing Liu
Guest Editors
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Keywords
- NMR spectroscopy
- advances in NMR techniques
- protein structure
- protein dynamics
- protein–ligand interaction
- large biomolecular complexes
- membrane proteins
- structure-based drug discovery
- in-cell NMR
- drug discovery
- 19F NMR
- chemical biology
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