A de Novo-Designed Monomeric, Compact Three-Helix-Bundle Protein on a Carbohydrate Template. Malik, L.; Nygaard, J.; Cristensen, N. J.; Madsen, C. S.; Rosner, H. I.; Kragelund, B. B.; Hoiberg-Nielsen, R.; Streicher, W. W.; Arleth, L.; Thulstrup, P. W.; and Jensen, K. J. CHEMBIOCHEM, 16(13):1905-1918, SEP 7, 2015.
doi  abstract   bibtex   
De novo design and chemical synthesis of proteins and of other artificial structures that mimic them is a central strategy for understanding protein folding and for accessing proteins with new functions. We have previously described carbohydrates that act as templates for the assembly of artificial proteins, so-called carboproteins. The hypothesis is that the template preorganizes the secondary structure elements and directs the formation of a tertiary structure, thus achieving structural economy in the combination of peptide, linker, and template. We speculate that the structural information from the template could facilitate protein folding. Here we report the design and synthesis of three-helix-bundle carboproteins on deoxyhexopyranosides. The carboproteins were analyzed by CD, analytical ultracentrifugation (AUC), small-angle X-ray scattering (SAXS), and NMR spectroscopy, and this revealed the formation of the first compact and folded monomeric carboprotein, distinctly different from a molten globule. En route to this carboprotein we observed a clear effect originating from the template on protein folding.
@article{ISI:000360492500012,
	Abstract = {{De novo design and chemical synthesis of proteins and of other
   artificial structures that mimic them is a central strategy for
   understanding protein folding and for accessing proteins with new
   functions. We have previously described carbohydrates that act as
   templates for the assembly of artificial proteins, so-called
   carboproteins. The hypothesis is that the template preorganizes the
   secondary structure elements and directs the formation of a tertiary
   structure, thus achieving structural economy in the combination of
   peptide, linker, and template. We speculate that the structural
   information from the template could facilitate protein folding. Here we
   report the design and synthesis of three-helix-bundle carboproteins on
   deoxyhexopyranosides. The carboproteins were analyzed by CD, analytical
   ultracentrifugation (AUC), small-angle X-ray scattering (SAXS), and NMR
   spectroscopy, and this revealed the formation of the first compact and
   folded monomeric carboprotein, distinctly different from a molten
   globule. En route to this carboprotein we observed a clear effect
   originating from the template on protein folding.}},
	Author = {Malik, Leila and Nygaard, Jesper and Cristensen, Niels J. and Madsen, Charlotte S. and Rosner, Heike I. and Kragelund, Birthe B. and Hoiberg-Nielsen, Rasmus and Streicher, Werner W. and Arleth, Lise and Thulstrup, Peter W. and Jensen, Knud J.},
	Date-Added = {2017-10-03 14:11:19 +0000},
	Date-Modified = {2017-10-03 14:11:19 +0000},
	Doi = {{10.1002/cbic.201500285}},
	Eissn = {{1439-7633}},
	Issn = {{1439-4227}},
	Journal = {{CHEMBIOCHEM}},
	Month = {{SEP 7}},
	Number = {{13}},
	Orcid-Numbers = {{Jensen, Knud/0000-0003-3525-5452 Thulstrup, Peter/0000-0002-9241-4352 Christensen, Niels Johan/0000-0001-9588-2656 Arleth, Lise/0000-0002-4694-4299}},
	Pages = {{1905-1918}},
	Researcherid-Numbers = {{Jensen, Knud/D-1145-2016 Thulstrup, Peter/C-5598-2013 Christensen, Niels Johan/J-3820-2014 }},
	Title = {{A de Novo-Designed Monomeric, Compact Three-Helix-Bundle Protein on a Carbohydrate Template}},
	Unique-Id = {{ISI:000360492500012}},
	Volume = {{16}},
	Year = {{2015}},
	Bdsk-Url-1 = {http://dx.doi.org/10.1002/cbic.201500285%7D}}
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