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Air oxidation method employed for the disulfide bond formation of natural and synthetic peptides

Air oxidation method employed for the disulfide bond formation of natural and synthetic peptides

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_1718975865

Air oxidation method employed for the disulfide bond formation of natural and synthetic peptides

About this item

Full title

Air oxidation method employed for the disulfide bond formation of natural and synthetic peptides

Publisher

Vienna: Springer Vienna

Journal title

Amino acids, 2015-08, Vol.47 (8), p.1507-1515

Language

English

Formats

Publication information

Publisher

Vienna: Springer Vienna

More information

Scope and Contents

Contents

Among the available protocols, chemically driven approaches to oxidize cysteine may not be required for molecules that, under the native-like conditions, naturally fold in conformations ensuring an effective pairing of the right disulfide bridge pattern. In this contest, we successfully prepared the distinctin, a natural heterodimeric peptide, and...

Alternative Titles

Full title

Air oxidation method employed for the disulfide bond formation of natural and synthetic peptides

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_1718975865

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_1718975865

Other Identifiers

ISSN

0939-4451

E-ISSN

1438-2199

DOI

10.1007/s00726-015-1983-4

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