BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

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Entry ID Data summary Entry Title Citation Title Authors
27075 Chemical Shifts: 1 set
1H and 15N Chemical Shift Assignments for phosphorylated S129 alpha-synuclein Exploring the role of post-translational modifications in regulating alpha-synuclein interactions by studying the effects of phosphorylation on nanobody binding Download bibtex for citation iamge Anass Chiki, Anthony Mittermaier, Bruno Fauvet, Christopher M Dobson, Erwin De Genst, Farah El Turk, Hilal A Lashuel, Justin Di Trani, Michele Vendruscolo, Mirva Hejjaoui, Tim Guilliams
27076 Chemical Shifts: 1 set
1H and 15N Chemical Shift Assignments for Y133F/Y136F mutant alpha-synuclein Exploring the role of post-translational modifications in regulating alpha-synuclein interactions by studying the effects of phosphorylation on nanobody binding Download bibtex for citation iamge Anass Chiki, Anthony Mittermaier, Bruno Fauvet, Christopher M Dobson, Erwin De Genst, Farah El Turk, Hilal A Lashuel, Justin Di Trani, Michele Vendruscolo, Mirva Hejjaoui, Tim Guilliams
27077 Chemical Shifts: 1 set
1H and 15N Chemical Shift Assignments for phosphorylated Y125, Y133F/Y136F mutant alpha-synuclein Exploring the role of post-translational modifications in regulating alpha-synuclein interactions by studying the effects of phosphorylation on nanobody binding Download bibtex for citation iamge Anass Chiki, Anthony Mittermaier, Bruno Fauvet, Christopher M Dobson, Erwin De Genst, Farah El Turk, Hilal A Lashuel, Justin Di Trani, Michele Vendruscolo, Mirva Hejjaoui, Tim Guilliams
27074 Chemical Shifts: 1 set
1H and 15N Chemical Shift Assignments for wild-type alpha-synuclein Exploring the role of post-translational modifications in regulating alpha-synuclein interactions by studying the effects of phosphorylation on nanobody binding Download bibtex for citation iamge Anass Chiki, Anthony Mittermaier, Bruno Fauvet, Christopher M Dobson, Erwin De Genst, Farah El Turk, Hilal A Lashuel, Justin Di Trani, Michele Vendruscolo, Mirva Hejjaoui, Tim Guilliams
25025 Chemical Shifts: 1 set
Heteronuclear NOE Values: 3 sets
T1 Relaxation Values: 4 sets
T2 Relaxation Values: 4 sets
Order Parameters: 2 sets
Conformational Plasticity Surrounding the Active Site of NADH Oxidase from Thermus thermophilus Conformational plasticity surrounding the active site of NADH oxidase from Thermus thermophilus Download bibtex for citation iamge Anthony Mittermaier, Justin Di Trani, Louis-Charles C Levros, Teresa Miletti