Towards Biomolecular Structure Determination by High-Resolution Solid-State NMR: Assignment of Solid Peptides
High-resolution solid-state NMR is rapidly evolving into a tool for determining the structure of biomolecules in solid phase, thereby opening up avenues for studying systems which are difficult to access by other methods. In this contribution, we focus on assigning the resonances of a unif...
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Format: | Article |
Language: | deu |
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Swiss Chemical Society
2001-10-01
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Series: | CHIMIA |
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Online Access: | https://www.chimia.ch/chimia/article/view/3497 |
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author | Andreas Detken Matthias Ernst Beat H. Meier |
author_facet | Andreas Detken Matthias Ernst Beat H. Meier |
author_sort | Andreas Detken |
collection | DOAJ |
description |
High-resolution solid-state NMR is rapidly evolving into a tool for determining the structure of biomolecules in solid phase, thereby opening up avenues for studying systems which are difficult to access by other methods. In this contribution, we focus on assigning the resonances of
a uniformly isotope-enriched peptide or protein to its primary structure. This represents a first step towards the goal of determining the complete three-dimensional structure of proteins by solid-state NMR. The assignment strategy relies on polarization-transfer experiments involving 13C
and 15N spins. The prospects for structural studies based on such assignments are discussed.
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first_indexed | 2024-12-13T03:30:04Z |
format | Article |
id | doaj.art-9ec64e77ef824bbbb2c2329e099e72e4 |
institution | Directory Open Access Journal |
issn | 0009-4293 2673-2424 |
language | deu |
last_indexed | 2024-12-13T03:30:04Z |
publishDate | 2001-10-01 |
publisher | Swiss Chemical Society |
record_format | Article |
series | CHIMIA |
spelling | doaj.art-9ec64e77ef824bbbb2c2329e099e72e42022-12-22T00:01:11ZdeuSwiss Chemical SocietyCHIMIA0009-42932673-24242001-10-015510Towards Biomolecular Structure Determination by High-Resolution Solid-State NMR: Assignment of Solid PeptidesAndreas DetkenMatthias ErnstBeat H. Meier High-resolution solid-state NMR is rapidly evolving into a tool for determining the structure of biomolecules in solid phase, thereby opening up avenues for studying systems which are difficult to access by other methods. In this contribution, we focus on assigning the resonances of a uniformly isotope-enriched peptide or protein to its primary structure. This represents a first step towards the goal of determining the complete three-dimensional structure of proteins by solid-state NMR. The assignment strategy relies on polarization-transfer experiments involving 13C and 15N spins. The prospects for structural studies based on such assignments are discussed. https://www.chimia.ch/chimia/article/view/3497AssignmentPolarization transferSolid-state nmr |
spellingShingle | Andreas Detken Matthias Ernst Beat H. Meier Towards Biomolecular Structure Determination by High-Resolution Solid-State NMR: Assignment of Solid Peptides CHIMIA Assignment Polarization transfer Solid-state nmr |
title | Towards Biomolecular Structure Determination by High-Resolution Solid-State NMR: Assignment of Solid Peptides |
title_full | Towards Biomolecular Structure Determination by High-Resolution Solid-State NMR: Assignment of Solid Peptides |
title_fullStr | Towards Biomolecular Structure Determination by High-Resolution Solid-State NMR: Assignment of Solid Peptides |
title_full_unstemmed | Towards Biomolecular Structure Determination by High-Resolution Solid-State NMR: Assignment of Solid Peptides |
title_short | Towards Biomolecular Structure Determination by High-Resolution Solid-State NMR: Assignment of Solid Peptides |
title_sort | towards biomolecular structure determination by high resolution solid state nmr assignment of solid peptides |
topic | Assignment Polarization transfer Solid-state nmr |
url | https://www.chimia.ch/chimia/article/view/3497 |
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