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Sequence, structure, and cooperativity in folding of elementary protein structural motifs

Sequence, structure, and cooperativity in folding of elementary protein structural motifs

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_1704124174

Sequence, structure, and cooperativity in folding of elementary protein structural motifs

About this item

Full title

Sequence, structure, and cooperativity in folding of elementary protein structural motifs

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2015-08, Vol.112 (32), p.9890-9895

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

Residue-level unfolding of two helix-turn-helix proteins—one naturally occurring and one de novo designed—is reconstructed from multiple sets of site-specific13C isotopically edited infrared (IR) and circular dichroism (CD) data using Ising-like statistical-mechanical models. Several model variants are parameterized to test the importance of sequen...

Alternative Titles

Full title

Sequence, structure, and cooperativity in folding of elementary protein structural motifs

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_journals_1704124174

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_1704124174

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.1506309112

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