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Biological Magnetic Resonance Data BankA Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules |
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Entry ID | Data summary | Entry Title | Citation Title | Authors |
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34621 | Chemical Shifts: 1 set Spectral_peak_list: 1 set |
NMR structure of the Bak transmembrane helix in DPC micelles |
High-resolution analysis of the conformational transition of pro-apoptotic Bak at the lipid membrane
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A Schiller, F Hagn, F Ruhrnossl, L E Sperl, M Haslbeck |
34622 | Chemical Shifts: 1 set Spectral_peak_list: 1 set |
NMR structure of the Bak transmembrane helix in lipid nanodiscs |
High-resolution analysis of the conformational transition of pro-apoptotic Bak at the lipid membrane
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A Schiller, F Hagn, F Ruhrnossl, L E Sperl, M Haslbeck |
30077 | Chemical Shifts: 1 set |
Structural model of a apo G-protein alpha subunit determined with NMR residual dipolar couplings and SAXS |
Conformational dynamics of a G-protein alpha subunit is tightly regulated by nucleotide binding
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A Plueckthun, D Goricanec, F Hagn, G Wagner, P Egloff, R Stehle, S Grigori |
30078 | Chemical Shifts: 1 set |
Structural Model of a Protein alpha subunit in complex with GDP obtained with SAXS and NMR residual couplings |
Conformational dynamics of a G-protein alpha subunit is tightly regulated by nucleotide binding
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A Plueckthun, D Goricanec, F Hagn, G Wagner, P Egloff, R Stehle, S Grigoriu |