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Optimization and validation of multi-state NMR protein structures using structural correlations

Optimization and validation of multi-state NMR protein structures using structural correlations

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9018667

Optimization and validation of multi-state NMR protein structures using structural correlations

About this item

Full title

Optimization and validation of multi-state NMR protein structures using structural correlations

Publisher

Dordrecht: Springer Netherlands

Journal title

Journal of biomolecular NMR, 2022-04, Vol.76 (1-2), p.39-47

Language

English

Formats

Publication information

Publisher

Dordrecht: Springer Netherlands

More information

Scope and Contents

Contents

Recent advances in the field of protein structure determination using liquid-state NMR enable the elucidation of multi-state protein conformations that can provide insight into correlated and non-correlated protein dynamics at atomic resolution. So far, NMR-derived multi-state structures were typically evaluated by means of visual inspection of str...

Alternative Titles

Full title

Optimization and validation of multi-state NMR protein structures using structural correlations

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9018667

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9018667

Other Identifiers

ISSN

0925-2738

E-ISSN

1573-5001

DOI

10.1007/s10858-022-00392-2

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