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Interplay among side chain sequence, backbone composition, and residue rigidification in polypeptide...

Interplay among side chain sequence, backbone composition, and residue rigidification in polypeptide...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_201390702

Interplay among side chain sequence, backbone composition, and residue rigidification in polypeptide folding and assembly

About this item

Full title

Interplay among side chain sequence, backbone composition, and residue rigidification in polypeptide folding and assembly

Publisher

United States: National Academy of Sciences

Journal title

Proceedings of the National Academy of Sciences - PNAS, 2008-07, Vol.105 (27), p.9151-9156

Language

English

Formats

Publication information

Publisher

United States: National Academy of Sciences

More information

Scope and Contents

Contents

The extent to which polypeptide conformation depends on side-chain composition and sequence has been widely studied, but less is known about the importance of maintaining an α-amino acid backbone. Here, we examine a series of peptides with backbones that feature different repeating patterns of α- and β-amino acid residues but an invariant side-chai...

Alternative Titles

Full title

Interplay among side chain sequence, backbone composition, and residue rigidification in polypeptide folding and assembly

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_journals_201390702

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_201390702

Other Identifiers

ISSN

0027-8424

E-ISSN

1091-6490

DOI

10.1073/pnas.0801135105

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