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Design and synthesis of a-helical peptides and mimetics

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dc.contributor.authorGarner, James
dc.contributor.authorHarding, Margaret
dc.date.accessioned2015-12-10T22:28:49Z
dc.date.issued2007
dc.date.updated2015-12-09T09:51:07Z
dc.description.abstractThe α-helix is the most abundant secondary structural element in proteins and is an important structural domain for mediating protein-protein and protein-nucleic acid interactions. Strategies for the rational design and synthesis of α-helix mimetics hav
dc.identifier.issn1477-0520
dc.identifier.urihttp://hdl.handle.net/1885/54620
dc.publisherRoyal Society of Chemistry
dc.sourceOrganic and Biomolecular Chemistry
dc.subjectKeywords: Antifreeze solutions; Bioactivity; Nucleic acids; Synthesis (chemical); Antifreeze proteins; Mimetics; Protein nucleic acid interactions; Rational design; Peptides; amino acid; antifreeze protein; biomimetic material; cyclopeptide; hydrocarbon; peptide; a
dc.titleDesign and synthesis of a-helical peptides and mimetics
dc.typeJournal article
local.bibliographicCitation.issue22
local.bibliographicCitation.lastpage3720
local.bibliographicCitation.startpage3557
local.contributor.affiliationGarner, James, University of New South Wales
local.contributor.affiliationHarding, Margaret, Administrative Division, ANU
local.contributor.authoruidHarding, Margaret, u4044881
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.identifier.absfor030400 - MEDICINAL AND BIOMOLECULAR CHEMISTRY
local.identifier.ariespublicationU3488905xPUB306
local.identifier.citationvolume5
local.identifier.doi10.1039/b710425a
local.identifier.scopusID2-s2.0-35748977122
local.type.statusPublished Version

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