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High-Affinity α-Conotoxin PnIA Analogs Designed on the Basis of the Protein Surface Topography Metho...

High-Affinity α-Conotoxin PnIA Analogs Designed on the Basis of the Protein Surface Topography Metho...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5107951

High-Affinity α-Conotoxin PnIA Analogs Designed on the Basis of the Protein Surface Topography Method

About this item

Full title

High-Affinity α-Conotoxin PnIA Analogs Designed on the Basis of the Protein Surface Topography Method

Publisher

London: Nature Publishing Group UK

Journal title

Scientific reports, 2016-11, Vol.6 (1), p.36848-36848, Article 36848

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Despite some success for small molecules, elucidating structure–function relationships for biologically active peptides — the ligands for various targets in the organism — remains a great challenge and calls for the development of novel approaches. Some of us recently proposed the Protein Surface Topography (PST) approach, which benefits from a sim...

Alternative Titles

Full title

High-Affinity α-Conotoxin PnIA Analogs Designed on the Basis of the Protein Surface Topography Method

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5107951

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5107951

Other Identifiers

ISSN

2045-2322

E-ISSN

2045-2322

DOI

10.1038/srep36848

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