Cargando…

Isotope-Aided Methods for Biological NMR Spectroscopy: Past, Present, and Future

This chapter starts by providing a historical background of our research endeavors over the past half-century to develop various isotope-aided methods in biological NMR spectroscopy, since innovations bloom only on the rich ground cultivated by previous investigators. We then focused on the stereo-a...

Descripción completa

Detalles Bibliográficos
Autores principales: Kainosho, Masatsune, Miyanoiri, Yohei, Takeda, Mitsuhiro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7122432/
http://dx.doi.org/10.1007/978-981-10-5966-7_2
_version_ 1783515416977473536
author Kainosho, Masatsune
Miyanoiri, Yohei
Takeda, Mitsuhiro
author_facet Kainosho, Masatsune
Miyanoiri, Yohei
Takeda, Mitsuhiro
author_sort Kainosho, Masatsune
collection PubMed
description This chapter starts by providing a historical background of our research endeavors over the past half-century to develop various isotope-aided methods in biological NMR spectroscopy, since innovations bloom only on the rich ground cultivated by previous investigators. We then focused on the stereo-array isotope-labeling (SAIL) method, one of our recent accomplishments, which culminates the isotope-aided NMR technologies for structural studies of proteins from various aspects: accurate structural determinations of large proteins, elaboration for automated structural determination, highly efficient and versatile residue-selective methyl labeling with newly developed auxotrophic E. coli strains, large-amplitude slow-breathing motion (LASBM) as revealed by the aromatic ring flipping of the residues in ligand-binding interfaces, and applications of the deuterium-induced (13)C-NMR isotope shift to investigate the hydrogen exchange phenomena of side-chain polar groups. Meanwhile, the expected role of NMR spectroscopy has been rapidly shifting from structure determinations to dynamics studies of biologically interesting targets, such as membrane proteins and larger protein complexes. The dynamic aspects of protein–protein and protein–ligand interactions are closely related to their biological functions and can be efficiently studied by using proteins residue selectively labeled with amino acids bearing optimized labeling patterns, prepared by cellular expression. We are absolutely confident that biological NMR spectroscopy will continually develop with further innovations of isotope-labeling technologies in the coming era, featuring ultrahigh field spectrometers beyond 1 GHz.
format Online
Article
Text
id pubmed-7122432
institution National Center for Biotechnology Information
language English
publishDate 2017
record_format MEDLINE/PubMed
spelling pubmed-71224322020-04-06 Isotope-Aided Methods for Biological NMR Spectroscopy: Past, Present, and Future Kainosho, Masatsune Miyanoiri, Yohei Takeda, Mitsuhiro Experimental Approaches of NMR Spectroscopy Article This chapter starts by providing a historical background of our research endeavors over the past half-century to develop various isotope-aided methods in biological NMR spectroscopy, since innovations bloom only on the rich ground cultivated by previous investigators. We then focused on the stereo-array isotope-labeling (SAIL) method, one of our recent accomplishments, which culminates the isotope-aided NMR technologies for structural studies of proteins from various aspects: accurate structural determinations of large proteins, elaboration for automated structural determination, highly efficient and versatile residue-selective methyl labeling with newly developed auxotrophic E. coli strains, large-amplitude slow-breathing motion (LASBM) as revealed by the aromatic ring flipping of the residues in ligand-binding interfaces, and applications of the deuterium-induced (13)C-NMR isotope shift to investigate the hydrogen exchange phenomena of side-chain polar groups. Meanwhile, the expected role of NMR spectroscopy has been rapidly shifting from structure determinations to dynamics studies of biologically interesting targets, such as membrane proteins and larger protein complexes. The dynamic aspects of protein–protein and protein–ligand interactions are closely related to their biological functions and can be efficiently studied by using proteins residue selectively labeled with amino acids bearing optimized labeling patterns, prepared by cellular expression. We are absolutely confident that biological NMR spectroscopy will continually develop with further innovations of isotope-labeling technologies in the coming era, featuring ultrahigh field spectrometers beyond 1 GHz. 2017-07-24 /pmc/articles/PMC7122432/ http://dx.doi.org/10.1007/978-981-10-5966-7_2 Text en © Springer Nature Singapore Pte Ltd. 2018 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Article
Kainosho, Masatsune
Miyanoiri, Yohei
Takeda, Mitsuhiro
Isotope-Aided Methods for Biological NMR Spectroscopy: Past, Present, and Future
title Isotope-Aided Methods for Biological NMR Spectroscopy: Past, Present, and Future
title_full Isotope-Aided Methods for Biological NMR Spectroscopy: Past, Present, and Future
title_fullStr Isotope-Aided Methods for Biological NMR Spectroscopy: Past, Present, and Future
title_full_unstemmed Isotope-Aided Methods for Biological NMR Spectroscopy: Past, Present, and Future
title_short Isotope-Aided Methods for Biological NMR Spectroscopy: Past, Present, and Future
title_sort isotope-aided methods for biological nmr spectroscopy: past, present, and future
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7122432/
http://dx.doi.org/10.1007/978-981-10-5966-7_2
work_keys_str_mv AT kainoshomasatsune isotopeaidedmethodsforbiologicalnmrspectroscopypastpresentandfuture
AT miyanoiriyohei isotopeaidedmethodsforbiologicalnmrspectroscopypastpresentandfuture
AT takedamitsuhiro isotopeaidedmethodsforbiologicalnmrspectroscopypastpresentandfuture