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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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19972 | Chemical Shifts: 1 set |
The proline-rich region of 18.5-kDa myelin basic protein requires long-range interactions with residues upstream to interact with the SH3-domain of Fyn |
The proline-rich region of 18.5 kDa myelin basic protein binds to the SH3-domain of Fyn tyrosine kinase with the aid of an upstream segment to form a dynamic complex in vitro
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George Harauz, Graham Smith, Kenrick A Vassall, Miguel De Avila, Vladimir V Bamm |
19949 | Chemical Shifts: 1 set T1 Relaxation Values: 1 set T2 Relaxation Values: 1 set |
The proline-rich region of 18.5-kDa myelin basic protein requires long-range interactions with residues upstream to interact with the SH3-domain of Fyn |
The proline-rich region of 18.5 kDa myelin basic protein binds to the SH3-domain of Fyn tyrosine kinase with the aid of an upstream segment to form a dynamic complex in vitro
|
George Harauz, Graham Smith, Kenrick A Vassall, Miguel De Avila, Vladimir V Bamm |
19948 | Chemical Shifts: 1 set T1 Relaxation Values: 1 set T2 Relaxation Values: 1 set |
The proline-rich region of 18.5-kDa myelin basic protein requires long-range interactions with residues upstream to interact with the SH3-domain of Fyn |
The proline-rich region of 18.5 kDa myelin basic protein binds to the SH3-domain of Fyn tyrosine kinase with the aid of an upstream segment to form a dynamic complex in vitro
|
George Harauz, Graham Smith, Kenrick A Vassall, Miguel De Avila, Vladimir V Bamm |
19186 | Chemical Shifts: 1 set |
Chemical shift assignments of a S72-S107 peptide of 18.5kDa murine myelin basic protein (MBP) |
The Effects of Threonine Phosphorylation on the Stability and Dynamics of the Central Molecular Switch Region of 18.5-kDa Myelin Basic Protein.
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Eugenia Polverini, George Harauz, Kenrick A Vassall, Kyrylo Bessonov, Miguel De Avila |
18520 | Chemical Shifts: 1 set |
Chemical shift assignments of a S72-S107 peptide of 18.5kDa murine myelin basic protein (MBP) in association with dodecylphosphocholine micelles |
Solution Nuclear Magnetic Resonance Structure and Molecular Dynamics Simulations of a Murine 18.5 kDa Myelin Basic Protein Segment (S72-S107) in Association with Dodecylphosphocholine Micelles.
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Eugenia Polverini, George Harauz, Kyrylo Bessonov, Miguel De Avila, Mumdooh AM Ahmed, Vladimir V Bamm |