Published February 26, 1996
| public
Journal Article
Structural Modification of a Periodic Polypeptide through Biosynthetic Replacement of Proline with Azetidine-2-carboxylic Acid
Abstract
Repetitive polypeptides comprising 16 repeats of the sequence -(AlaGly)_3ProGluGly- (1a) have been prepared from Escherichia coli as overexpressed recombinant proteins. Partial in vivo replacement of the proline (Pro) residues in sequence 1a with L-azetidine-2-carboxylic acid (Aze) was achieved by expression of the target protein in medium containing Aze and lacking Pro. NMR and amino acid analysis for residual proline in the polymer indicated 25-40% replacement of Pro by Aze. While polymers of 1a form conformationally disordered solids, incorporation of Aze allows this material to adopt a â-sheet structure in the solid state.
Additional Information
Copyright © 1996 American Chemical Society. Received July 24, 1995; Revised Manuscript Received November 29, 1995. Publication Date (Web): February 26, 1996. Abstract published in Advance ACS Abstracts, February 1, 1996. This work was supported by Contract No. DAAHO4-93-G-0217 from the U.S. Army Research Office and by a grant (DMR-8914359) from the Polymers and Genetics Programs of the National Science Foundation. T.J.D. acknowledges the National Institutes of Health for a National Research Service Award postdoctoral training fellowship. NMR spectra were recorded in the University of Massachusetts NMR Facility, which is supported in part by the NSF Materials Research Science and Engineering Center at the University. We thank Brian Price and Wendy Petka for assistance with electrophoretic analyses.Additional details
- Eprint ID
- 53473
- Resolver ID
- CaltechAUTHORS:DEMm1996
- Army Research Office (ARO)
- DAAHO4-93-G-0217
- NSF
- DMR-8914359
- NIH Postdoctoral Fellowship
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