Special Issue "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: 31 August 2022 | Viewed by 2463

Special Issue Editors

Prof. Dr. Chaowei Shi
E-Mail Website
Guest Editor
Hefei National Laboratory for Physical Sciences at the Microscale, University of Science and Technology of China, Hefei 230026, China
Interests: solid-state NMR; protein structure; conformational dynamics; membrane protein; ion channel; intramembrane protease; transporter
Prof. Dr. Lichun He
E-Mail Website
Guest Editor
Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan 430071, China
Interests: NMR; protein structure and dynamics; protein folding; protein–protein interactions; antibody and nanobody; membrane protein; chaperones
Prof. Dr. Yan Li
E-Mail Website
Guest Editor
Department of Pathogen Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China
Interests: NMR; structure biology; high-throughput screening; protein–ligand interaction; virus protein structure
Prof. Dr. Bing Liu
E-Mail Website
Guest Editor
Institute for Protein Science and Phage Research, Xi'an Jiaotong University, Xi'an 710061, China
Interests: solution NMR; cryo-EM; drug discovery; antibiotics; phage–host interaction; phage therapy

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

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Life is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

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

Published Papers (2 papers)

Order results
Result details
Select all
Export citation of selected articles as:

Research

Article
NMR Reveals the Conformational Changes of Cytochrome C upon Interaction with Cardiolipin
Life 2021, 11(10), 1031; https://doi.org/10.3390/life11101031 - 30 Sep 2021
Viewed by 857
Abstract
Conformational change of cytochrome c (cyt c) caused by interaction with cardiolipin (CL) is an important step during apoptosis, but the underlying mechanism is controversial. To comprehensively clarify the structural transformations of cyt c upon interaction with CL and avoid the unpredictable alias [...] Read more.
Conformational change of cytochrome c (cyt c) caused by interaction with cardiolipin (CL) is an important step during apoptosis, but the underlying mechanism is controversial. To comprehensively clarify the structural transformations of cyt c upon interaction with CL and avoid the unpredictable alias that might come from protein labeling or mutations, the conformation of purified yeast iso–1 cyt c with natural isotopic abundance in different contents of CL was measured by using NMR spectroscopy, in which the trimethylated group of the protein was used as a natural probe. The data demonstrate that cyt c has two partially unfolded conformations when interacted with CL: one with Fe–His33 coordination and the other with a penta–coordination heme. The Fe–His33 coordination conformation can be converted into a penta–coordination heme conformation in high content of CL. The structure of cyt c becomes partially unfolded with more exposed heme upon interaction with CL, suggesting that cyt c prefers a high peroxidase activity state in the mitochondria, which, in turn, makes CL easy to be oxidized, and causes the release of cyt c into the cytoplasm as a trigger in apoptosis. Full article
(This article belongs to the Special Issue Application of Nuclear Magnetic Resonance Method in Protein Research)
Show Figures

Figure 1

Article
Solid-State NMR Studies of the Succinate-Acetate Permease from Citrobacter Koseri in Liposomes and Native Nanodiscs
Life 2021, 11(9), 908; https://doi.org/10.3390/life11090908 - 31 Aug 2021
Viewed by 919
Abstract
The succinate-acetate permease (SatP) is an anion channel with six transmembrane domains. It forms different oligomers, especially hexamers in the detergent as well as in the membrane. Solid-state NMR studies of SatP were carried out successfully on SatP complexes by reconstructing the protein [...] Read more.
The succinate-acetate permease (SatP) is an anion channel with six transmembrane domains. It forms different oligomers, especially hexamers in the detergent as well as in the membrane. Solid-state NMR studies of SatP were carried out successfully on SatP complexes by reconstructing the protein into liposomes or retaining the protein in the native membrane of E. coli., where it was expressed. The comparison of 13C-13C 2D correlation spectra between the two samples showed great similarity, opening the possibility to further study the acetate transport mechanism of SatP in its native membrane environment. Solid-state NMR studies also revealed small chemical shift differences of SatP in the two different membrane systems, indicating the importance of the lipid environment in determining the membrane protein structures and dynamics. Combining different 2D SSNMR spectra, chemical shift assignments were made on some sites, consistent with the helical structures in the transmembrane domains. In the end, we pointed out the limitation in the sensitivity for membrane proteins with such a size, and also indicated possible ways to overcome it. Full article
(This article belongs to the Special Issue Application of Nuclear Magnetic Resonance Method in Protein Research)
Show Figures

Figure 1

Back to TopTop