Proline-poor hydrophobic domains modulate the assembly and material properties of polymeric elastin-Reference-Cited by-同舟云学术

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Proline-poor hydrophobic domains modulate the assembly and material properties of polymeric elastin

Published:2015-07-24 Issue:10 Volume:103 Page:563-573
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Muiznieks Lisa D.¹,Reichheld Sean E.¹,Sitarz Eva E.¹,Miao Ming¹,Keeley Fred W.¹²³

Affiliation:

1. Molecular Structure and Function Program, Research Institute, Hospital For Sick Children; 555 University Ave Toronto ON M5G1X8 Canada

2. Department of Biochemistry; University of Toronto; Toronto ON M5S1A8 Canada

3. Department of Laboratory Medicine and Pathobiology; University of Toronto; Toronto ON M5S1A8 Canada

Funder

Heart and Stroke Foundation of Canada

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/bip.22663/fullpdf

Reference33 articles.

1. Flexibility in the Solution Structure of Human Tropoelastin

2. Proline and Glycine Control Protein Self-Organization into Elastomeric or Amyloid Fibrils

3. Quantitative Observation of Backbone Disorder in Native Elastin

4. Conformational Transitions of the Cross-linking Domains of Elastin during Self-assembly

5. Proline Periodicity Modulates the Self-assembly Properties of Elastin-like Polypeptides

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