Artificial Protein Block Copolymers Blocks Comprising Two Distinct Self-Assembling Domains

It's the way that you do it: Block polymers composed of elastin (E) and COMPcc (C) domains (see figure) have been synthesised and characterised. The protein motifs were chosen for their structures and distinct self‐assembly modes. We demonstrate that the micro‐ and macrostructures of the polyme...

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Bibliographic Details
Published in:	Chembiochem : a European journal of chemical biology Vol. 10; no. 17; pp. 2733 - 2735
Main Authors:	Haghpanah, Jennifer S, Yuvienco, Carlo, Civay, Deniz E, Barra, Hanna, Baker, Peter J, Khapli, Sachin, Voloshchuk, Natalya, Gunasekar, Susheel K, Muthukumar, Murugappan, Montclare, Jin K
Format:	Journal Article
Language:	English
Published:	Weinheim Wiley-VCH Verlag 23-11-2009 WILEY-VCH Verlag WILEY‐VCH Verlag
Subjects:	alpha-helices Amino Acid Sequence biomaterials elastin Molecular Sequence Data Molecular Structure Polymers - chemical synthesis Polymers - chemistry Protein Conformation protein structures Proteins - chemistry Proteins - genetics self-assembly
Online Access:	Get full text
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Summary:	It's the way that you do it: Block polymers composed of elastin (E) and COMPcc (C) domains (see figure) have been synthesised and characterised. The protein motifs were chosen for their structures and distinct self‐assembly modes. We demonstrate that the micro‐ and macrostructures of the polymers are dictated by the orientation of the fusions and the number of repeated blocks.
Bibliography:	http://dx.doi.org/10.1002/cbic.200900539 AFOSR - No. FA-9550-07-1-0060; No. FA9550-07-1-0347 GK-12 Fellows - No. DGE-0741714 ArticleID:CBIC200900539 NSF MRSEC - No. DMR-0820341; No. DMR-0706454 ark:/67375/WNG-RSHHJ0CK-F istex:136C056804F54889209CDF15A94735EA5859B0E1 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1439-4227 1439-7633
DOI:	10.1002/cbic.200900539