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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Main Authors: Andreas Detken, Matthias Ernst, Beat H. Meier
Format: Article
Language:deu
Published: Swiss Chemical Society 2001-10-01
Series:CHIMIA
Subjects:
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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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
work_keys_str_mv AT andreasdetken towardsbiomolecularstructuredeterminationbyhighresolutionsolidstatenmrassignmentofsolidpeptides
AT matthiasernst towardsbiomolecularstructuredeterminationbyhighresolutionsolidstatenmrassignmentofsolidpeptides
AT beathmeier towardsbiomolecularstructuredeterminationbyhighresolutionsolidstatenmrassignmentofsolidpeptides