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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Published inChembiochem : 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
LanguageEnglish
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
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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
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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