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Correlated Dynamics of Consecutive Residues Reveal Transient and Cooperative Unfolding of Secondary...

Correlated Dynamics of Consecutive Residues Reveal Transient and Cooperative Unfolding of Secondary...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_crossref_primary_10_1073_pnas_0504361102

Correlated Dynamics of Consecutive Residues Reveal Transient and Cooperative Unfolding of Secondary Structure in Proteins

About this item

Full title

Correlated Dynamics of Consecutive Residues Reveal Transient and Cooperative Unfolding of Secondary Structure in Proteins

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2005-11, Vol.102 (47), p.16984-16989

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Nuclear spin relaxation is a powerful method for studying molecular dynamics at atomic resolution. Recent methods development in biomolecular NMR spectroscopy has enabled detailed investigations of molecular dynamics that are critical for biological function, with prominent examples addressing allostery, enzyme catalysis, and protein folding. Dynam...

Alternative Titles

Full title

Correlated Dynamics of Consecutive Residues Reveal Transient and Cooperative Unfolding of Secondary Structure in Proteins

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_crossref_primary_10_1073_pnas_0504361102

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_crossref_primary_10_1073_pnas_0504361102

Other Identifiers

ISSN

0027-8424,1091-6490

E-ISSN

1091-6490

DOI

10.1073/pnas.0504361102