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Solid State Conformational Transitions In Peptides Modeling B. Mori Fibroin

Published online by Cambridge University Press:  02 July 2020

D. Wilson ,
R. Valluzzi ,
T. Vuong ,
S-J Chien ,
S. P. Gido  and
D. Kaplan
D. Wilson
Affiliation:
Department of Chemical Engineering, Biotechnology Center, Tufts University, Medford, MA02155
R. Valluzzi
Affiliation:
Department of Chemical Engineering, Biotechnology Center, Tufts University, Medford, MA02155 Department of Polymer Science and Engineering, University of Massachusetts, Amherst, MA01003
T. Vuong
Affiliation:
Department of Polymer Science and Engineering, University of Massachusetts, Amherst, MA01003
S-J Chien
Affiliation:
Department of Polymer Science and Engineering, University of Massachusetts, Amherst, MA01003
S. P. Gido
Affiliation:
Department of Polymer Science and Engineering, University of Massachusetts, Amherst, MA01003
D. Kaplan
Affiliation:
Department of Chemical Engineering, Biotechnology Center, Tufts University, Medford, MA02155
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Extract

Fibrous proteins are molecules whose secondary structures are their dominant motifs due to their highly repetitive amino acid sequences. Most fibrous proteins have physiological roles as protective, connective or structural materials. Among the fibrous proteins, silks tend to have blocky structures, with crystallizable and amorphous blocks comprised of short, highly repetitive amino acid sequences. In addition, the high glycine content of silks allows them greater conformational variability than most proteins, thus Bombyx morisilk fibroin is typically polymorphic.

The ability of silk fibroin to adopt multiple conformations and crystal structures makes it difficult to obtain corroborating data using multiple characterization techniques. Differences in sample preparation to accommodate different techniques can also affect the resulting sample structure. Reproducible sample preparation was achieved for IR and TEM experiments by rubbing the dried IR sample with a carbon substrate TEM grid to pick up tiny flakes of solidified peptide.

Type
Biopolymers and Biomemetics
Information
Microscopy and Microanalysis , Volume 5 , Issue S2: Proceedings: Microscopy & Microanalysis '99, Microscopy Society of America 57th Annual Meeting, Microbeam Analysis Society 33rd Annual Meeting, Portland, Oregon August 1-5, 1999 , August 1999 , pp. 1216 - 1217
Copyright
Copyright © Microscopy Society of America

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References

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7) We would like to acknowledge support from the National Science Foundation; NSF DMR- 9708062 and NSF BES-9727401, the NSF MRSEC program, and from the W. M. Keck Foundation Biomimetic Materials and Polymer Morphology LaboratoriesGoogle Scholar