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Entry ID Original Release date Data summary Entry Title Citation Title Authors
27250 2018-03-08 Chemical Shifts: 1 set
CW domain of ASHH2 methyltransferase 1H, 13C, and 15N resonance assignments of CW domain of the N-methyltransferase ASHH2 free and bound to the mono-, di- and tri-methylated histone H3 tail peptides Download bibtex for citation iamge Maxim Brilkov, Olena Dobrovolska, Oyvind Halskau, Oyvind Odegard, Rein Aasland
27251 2018-03-08 Chemical Shifts: 1 set
Backbone and sidechain 1H, 13C, and 15N Chemical Shift Assignments for CW domain of Histone-lysine N-methyltransferase ASHH2 bound to H3K4me1 1H, 13C, and 15N resonance assignments of CW domain of the N-methyltransferase ASHH2 free and bound to the mono-, di- and tri-methylated histone H3 tail peptides Download bibtex for citation iamge Maxim Brilkov, Olena Dobrovolska, Oyvind Halskau, Oyvind Odegard, Rein Aasland
26892 2021-07-26 Chemical Shifts: 1 set
In solution NMR characterization of an engineered membrane active peptide, A-Cage-C Investigating the Disordered and Membrane-Active Peptide A-Cage-C Using Conformational Ensembles Download bibtex for citation iamge age Aleksander A Skjevik, Knut Teigen, Martin Jakubec, Morten L Govasli, Nils age a Froystein, Olena Dobrovolska, Orjan Sele S Handegard, Oyvind Halskau, Oyvind StrOmland
17888 2012-08-17 Chemical Shifts: 1 set
NMR Structure of the Polyserine Tract of Apis mellifera Vitellogenin, residues 358-392 A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation Download bibtex for citation iamge Florian Wolschin, Gro V Amdam, Heli Havukainen, Jarl Underhaug, Oyvind Halskau
17889 2012-05-22 Chemical Shifts: 1 set
The polyserine tract of Nasonia vitripennis Vg residues 351-385 A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation. Download bibtex for citation iamge Florian Wolschin, Gro Amdam, Heli Havukainen, Jarl Underhaug, Oyvind Halskau