| Entry ID |
Data summary |
Entry Title |
Citation Title |
Authors |
| 27250 |
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 |
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 |
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 |
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 |
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 |
