Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Linde E. J. Smeenk"'
Autor:
Joris J. Benschop, Wouter Cornelis Puijk, Drohpatie Timmers‐Parohi, Peter Timmerman, Henk Hiemstra, Linde E. J. Smeenk, Jan H. van Maarseveen
Publikováno v:
ChemBioChem, 16(1), 91-99. Wiley-VCH Verlag
Making peptide-based molecules that mimic functional interaction sites on proteins remains a challenge in biomedical sciences. Here, we present a robust technology for the covalent assembly of highly constrained and discontinuous binding site mimics,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db7c383806dff437d3a5a96e4d4dc7f3
https://dare.uva.nl/personal/pure/en/publications/reconstructing-the-discontinuous-and-conformational-1-3loop-binding-site-on-hfshhcg-by-using-highly-constrained-multicyclic-peptides(a4044ab4-e2dd-4604-bd2f-b579078c11e5).html
https://dare.uva.nl/personal/pure/en/publications/reconstructing-the-discontinuous-and-conformational-1-3loop-binding-site-on-hfshhcg-by-using-highly-constrained-multicyclic-peptides(a4044ab4-e2dd-4604-bd2f-b579078c11e5).html
Autor:
Kristen A. Marino, Albert J Kettelarij, Matthijs R. Panman, Heleen Meuzelaar, Linde E. J. Smeenk, Peter Timmerman, Adriana Huerta-Viga, Jan H. van Maarseveen, Peter G. Bolhuis, Sander Woutersen
Publikováno v:
The journal of Physical Chemistry. B, 117(39), 11490-11501. American Chemical Society
The Journal of Physical Chemistry B
The Journal of Physical Chemistry B
Trp-cage is a synthetic 20-residue miniprotein which folds rapidly and spontaneously to a well-defined globular structure more typical of larger proteins. Due to its small size and fast folding, it is an ideal model system for experimental and theore
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58447940573be872c11876565950c85b
https://doi.org/10.1021/jp404714c
https://doi.org/10.1021/jp404714c
Autor:
Leo J. de Koning, Luitzen de Jong, Jeremy M. Baskin, Chris G. de Koster, Linde E. J. Smeenk, JaapWillem Back, Gert Jan Kramer, Jan H. van Maarseveen, Merel A. Nessen, Henk Hiemstra, Carolyn R. Bertozzi
Publikováno v:
Journal of Proteome Research, 8(7), 3702-3711. American Chemical Society
Journal of proteome research, 8, 3702-3711. American Chemical Society
Journal of proteome research, 8, 3702-3711. American Chemical Society
A general method is described to sequester peptides containing azides from complex peptide mixtures, aimed at facilitating mass spectrometric analysis to study different aspects of proteome dynamics. The enrichment method is based on covalent capture
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1696af41f935f7b0dac6cfa19750bbb
https://doi.org/10.1021/pr900257z
https://doi.org/10.1021/pr900257z
Publikováno v:
Organic Letters, 14(5), 1194-1197. American Chemical Society
The synthesis and applications of water-soluble scaffolds that conformationally constrain side chain unprotected linear peptides containing two cysteines are described. These scaffolds contain a functionality with orthogonal reactivity to be used for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::996071ee750a30aeeb5897fbcd012989
https://pubmed.ncbi.nlm.nih.gov/22332901
https://pubmed.ncbi.nlm.nih.gov/22332901
Autor:
Drohpatie Timmers‐Parohi, Linde E. J. Smeenk, Joris J. Benschop, Wouter Cornelis Puijk, Henk Hiemstra, Jan H. van Maarseveen, Peter Timmerman
Publikováno v:
ChemBioChem. 16:1-1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1d3896b5144190017b98481b730987e9
https://doi.org/10.1002/cbic.201490067
https://doi.org/10.1002/cbic.201490067