In:
Science, American Association for the Advancement of Science (AAAS), Vol. 293, No. 5530 ( 2001-07-27), p. 676-680
Abstract:
Polymerization of isocyanopeptides results in the formation of high molecular mass polymers that fold in a proteinlike fashion to give helical strands in which the peptide chains are arranged in β-sheets. The β-helical polymers retain their structure in water and unfold in a cooperative process at elevated temperatures. The peptide architecture in these polymers is a different form of the β-helix motif found in proteins. Unlike their natural counterparts, which contain arrays of large β-sheets stacked in a helical fashion, the isocyanopeptide polymers have a central helical core that acts as a director for the β-sheet–like arrangement of the peptide side arms. The helical structure of these isocyanopeptide polymers has the potential to be controlled through tailoring of the side branches and the hydrogen-bonding network present in the β-sheets.
Type of Medium:
Online Resource
ISSN:
0036-8075
,
1095-9203
DOI:
10.1126/science.1062224
Language:
English
Publisher:
American Association for the Advancement of Science (AAAS)
Publication Date:
2001
detail.hit.zdb_id:
128410-1
detail.hit.zdb_id:
2066996-3
detail.hit.zdb_id:
2060783-0
SSG:
11
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