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Biomolecular NMR Spectroscopy

A special issue of Molecules (ISSN 1420-3049).

Deadline for manuscript submissions: closed (15 September 2021) | Viewed by 5164

Special Issue Editors

Institute for Molecular Bioscience, University of Queensland, St Lucia, QLD, Australia
Interests: peptides; proteins; peptide–protein interactions; biomolecular dynamics and structure; solution-state NMR; drug design
Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Melbourne, Australia
Interests: biophysics; solid state NMR; in-cell NMR; biological membrane; toxins; antimicrobial peptides; amyloid peptides
Centre for Advanced Imaging, University of Queensland, St Lucia, QLD, Australia
Interests: peptides; animal toxins; proteins; biomolecular NMR; solution-state NMR; protein structural biology; ion channel research; isotopic labeling

Special Issue Information

Dear Colleagues,

NMR is a non-invasive technique that can provide invaluable structural information on complex molecular organizations. It is one of the most powerful techniques in structural biology research that can deliver explicit information on protein architecture and dynamics. This information advances our understanding of complex biological mechanisms and provides guidance for drug design and development. Recent advancements in NMR methods and instrumentation have enabled structure determination of large biomolecules (including protein complexes) and the study of these biomolecules in complex cellular environments. The recent development of NMR methods to carry out in situ study of cell membrane constituents, i.e., lipids, small molecules, proteins, and peptides, is also providing exciting insights into cellular research.

This Special Issue will highlight the methodology and applications used to study the structure of proteins, peptides, and biological membranes. In addition to structural studies, we aim to include studies of membrane interactions, molecular motions, and novel NMR methods. Overall, this Special Issue will provide the reader with a broad overview of the newest advances in the field and an appreciation of the power of NMR in studying complex biomolecular systems.


Prof. Dr. Marc Antoine Sani
Dr. Yanni Chin
Dr. Conan Wang
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. Molecules is an international peer-reviewed open access semimonthly 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 2700 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

  • solution-state NMR
  • solid-state NMR
  • structural biology
  • proteins
  • peptides
  • protein complexes
  • lipid membranes
  • protein dynamics
  • drug design
  • in-cell NMR
  • method development

Published Papers (2 papers)

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Research

14 pages, 2391 KiB  
Article
Insight into Functional Membrane Proteins by Solution NMR: The Human Bcl-2 Protein—A Promising Cancer Drug Target
by Ameeq Ul Mushtaq, Jörgen Ådén, Tobias Sparrman, Mattias Hedenström and Gerhard Gröbner
Molecules 2021, 26(5), 1467; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules26051467 - 08 Mar 2021
Cited by 1 | Viewed by 2448
Abstract
Evasion from programmed cell death (apoptosis) is the main hallmark of cancer and a major cause of resistance to therapy. Many tumors simply ensure survival by over-expressing the cell-protecting (anti-apoptotic) Bcl-2 membrane protein involved in apoptotic regulation. However, the molecular mechanism by which [...] Read more.
Evasion from programmed cell death (apoptosis) is the main hallmark of cancer and a major cause of resistance to therapy. Many tumors simply ensure survival by over-expressing the cell-protecting (anti-apoptotic) Bcl-2 membrane protein involved in apoptotic regulation. However, the molecular mechanism by which Bcl-2 protein in its mitochondrial outer membrane location protects cells remains elusive due to the absence of structural insight; and current strategies to therapeutically interfere with these Bcl-2 sensitive cancers are limited. Here, we present an NMR-based approach to enable structural insight into Bcl-2 function; an approach also ideal as a fragment-based drug discovery platform for further identification and development of promising molecular Bcl-2 inhibitors. By using solution NMR spectroscopy on fully functional intact human Bcl-2 protein in a membrane-mimicking micellar environment, and constructs with specific functions remaining, we present a strategy for structure determination and specific drug screening of functional subunits of the Bcl-2 protein as targets. Using 19F NMR and a specific fragment library (Bionet) with fluorinated compounds we can successfully identify various binders and validate our strategy in the hunt for novel Bcl-2 selective cancer drug strategies to treat currently incurable Bcl-2 sensitive tumors. Full article
(This article belongs to the Special Issue Biomolecular NMR Spectroscopy)
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15 pages, 3479 KiB  
Article
Novel NMR Assignment Strategy Reveals Structural Heterogeneity in Solution of the nsP3 HVD Domain of Venezuelan Equine Encephalitis Virus
by Peter Agback, Andrey Shernyukov, Francisco Dominguez, Tatiana Agback and Elena I. Frolova
Molecules 2020, 25(24), 5824; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules25245824 - 10 Dec 2020
Cited by 5 | Viewed by 2021
Abstract
In recent years, intrinsically disordered proteins (IDPs) and disordered domains have attracted great attention. Many of them contain linear motifs that mediate interactions with other factors during formation of multicomponent protein complexes. NMR spectrometry is a valuable tool for characterizing this type of [...] Read more.
In recent years, intrinsically disordered proteins (IDPs) and disordered domains have attracted great attention. Many of them contain linear motifs that mediate interactions with other factors during formation of multicomponent protein complexes. NMR spectrometry is a valuable tool for characterizing this type of interactions on both amino acid (aa) and atomic levels. Alphaviruses encode a nonstructural protein nsP3, which drives viral replication complex assembly. nsP3 proteins contain over 200-aa-long hypervariable domains (HVDs), which exhibits no homology between different alphavirus species, are predicted to be intrinsically disordered and appear to be critical for alphavirus adaptation to different cells. Previously, we have shown that nsP3 HVD of chikungunya virus (CHIKV) is completely disordered with low tendency to form secondary structures in free form. In this new study, we used novel NMR approaches to assign the spectra for the nsP3 HVD of Venezuelan equine encephalitis virus (VEEV). The HVDs of CHIKV and VEEV have no homology but are both involved in replication complex assembly and function. We have found that VEEV nsP3 HVD is also mostly disordered but contains a short stable α-helix in its C-terminal fragment, which mediates interaction with the members of cellular Fragile X syndrome protein family. Our NMR data also suggest that VEEV HVD has several regions with tendency to form secondary structures. Full article
(This article belongs to the Special Issue Biomolecular NMR Spectroscopy)
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