Published November 1993
| public
Journal Article
Determination of the chain-folding pattern in the crystalline domains of the repetitive polypeptide {(AlaGly)_3GluGly(GlyAla)_3GluGly}_10 by FTIR studies of its blends with a ^(13)C-enriched analog
Abstract
We are interested in the design and characterization of repetitive polypeptides that assemble into lamellae of uniform, predetermined thickness (Figure 1). In the initial stages of this work, the design of the polypeptide repeating unit (which comprises a sequence of amino acids traversing the thickness of the lamella and a turn sequence) has been based in part on work on the structure of silk and its analogues and in part on the literature on reverse turns in globular protein. In particular, we have reported the synthesis and characterization of polypeptides comprising repeating unit sequences 1-3.
Additional Information
© 1993 American Chemical Society. Received August 23, 1993; Revised Manuscript Received September 27, 1993. This work was supported by grants from Polymers and Genetics Programs of the National Science Foundation and by the NSF Materials Research Laboratory at the University of Massachusetts. We thank P. T. Lansbury (Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA) and S. L. Hsu (Department of Polymer Science and Engineering, University of Massachusetts, Amherst, MA) for discussions regarding FTIR spectroscopy.Additional details
- Alternative title
- Determination of the chain-folding pattern in the crystalline domains of the repetitive polypeptide {(AlaGly)3GluGly(GlyAla)3GluGly}10 by FTIR studies of its blends with a carbon-13 enriched analog
- Eprint ID
- 53494
- Resolver ID
- CaltechAUTHORS:PARm1993
- NSF
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