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
|
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
|
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
|
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
|
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.
|
Florian Wolschin, Gro Amdam, Heli Havukainen, Jarl Underhaug, Oyvind Halskau |